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Showing drug card for Cefalotin (DB00456)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:00
Primary Accession Number DB00456
Secondary Accession Number
  • APRD00859
  • EXPT00946
Name Cefalotin
Drug Type
  • Approved
  • Small Molecule
Description A cephalosporin antibiotic. [PubChem]
Synonyms
  1. CLS
  2. Cefalothin
  3. Cefalotina [INN-Spanish]
  4. Cefalotine [INN-French]
  5. Cefalotinum [INN-Latin]
  6. Cephalothin
  7. Cephalothin Sodium
  8. Cephalothinum
  9. Cephalotin
Brand Names
  1. Averon-1
  2. Cemastin
  3. Coaxin
  4. Keflin
  5. Seffin
Brand Mixtures Not Available
Chemical IUPAC Name (6R,7R)-3-(acetyloxymethyl)-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Chemical Formula C16H16N2O6S2
Chemical Structure Structure
CAS Registry Number 153-61-7
InChI Identifier InChI=1/C16H16N2O6S2/c1-8(19)24-6-9-7-26-15-12(14(21)18(15)13(9)16(22)23)17-11(20)5-10-3-2-4-25-10/h2-4,12,15H,5-7H2,1H3,(H,17,20)(H,22,23)/t12-,15-/m1/s1/f/h17,22H
InChI Key XIURVHNZVLADCM-OQJUERBUDY
KEGG Drug Not Available
KEGG Compound C07761 Link Image
PubChem Compound 6024 Link Image
PubChem Substance 9963 Link Image
ChEBI ID Not Available
PharmGKB ID PA448886 Link Image
HET ID CEO Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02060051 Link Image
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Cefalotin Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 396.4380
Monoisotopic Molecular Weight 396.0450
State Solid
Melting Point 160-160.5 oC
Experimental Water Solubility 158 mg/L Source: PhysProp
Predicted Water Solubility 5.21e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.2 Source: PhysProp
Predicted LogP 0.63 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.88 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1CEG Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC(=O)OCC1=C(N2[C@H](SC1)[C@H](NC(=O)CC1=CC=CS1)C2=O)C(O)=O
Canonical SMILES CC(=O)OCC1=C(N2C(SC1)C(NC(=O)CC1=CC=CS1)C2=O)C(O)=O
Drug Category
  • Anti-Bacterial Agents
  • Cephalosporins
ATC Codes
AHFS Codes
  • 08:12.06.04
Indication Used to prevent infection during surgery and to treat many kinds of infections of the blood, bone or joints, respiratory tract, skin, and urinary tract.
Pharmacology Cefalotin (INN) or cephalothin (USAN) is a semisynthetic first generation cephalosporin having a broad spectrum of antibiotic activity that is administered parenterally.
Mechanism of Action The bactericidal activity of cefalotin results from the inhibition of cell wall synthesis via affinity for penicillin-binding proteins (PBPs).
Absorption Not Available
Toxicity Rat intravenous LD50 is 4000 mg/kg.
Protein Binding 65-80%
Biotransformation Metabolized to a less active desacetyl metabolite, although 50-75% of the drug is eliminated unchanged in the urine.
Half Life 30 minutes
Dosage Forms
Form Route
Powder, for solution Intravenous
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Serum albumin
  2. Penicillin-binding proteins 1A/1B
  3. Endosialin
  4. D-alanyl-D-alanine carboxypeptidase
  5. Beta-lactamase
Drug Target 1 [top]
Target 1 ID 587
Target 1 Name Serum albumin
Target 1 Synonyms
  1. Serum albumin precursor
Target 1 Gene Name ALB
Target 1 Protein Sequence >Serum albumin precursor
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Target 1 Number of Residues 619
Target 1 Molecular Weight 69367
Target 1 Theoretical pI 6.21
Target 1 GO Classification
Function
transporter activity
carrier activity
Process
physiological process
cellular physiological process
transport
Component
extracellular region
extracellular space
Target 1 General Function Involved in antioxidant activity
Target 1 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-18
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 28590 Link Image
Target 1 UniProtKB/Swiss-Prot ID P02768 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Target 1 PDB ID 1HA2 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Secreted protein
Target 1 Gene Sequence >1830 bp
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ALB Link Image
Target 1 GenAtlas ID ALB Link Image
Target 1 HGNC ID HGNC:399 Link Image
Target 1 Chromosome Location 4
Target 1 Locus 4q11-q13
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  2. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  3. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  6. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  7. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  10. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  11. 1518850 Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9.
  12. 1630489 He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15.
  13. 1859851 Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54.
  14. 1946412 Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7.
  15. 2068071 Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63.
  16. 2104980 Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30.
  17. 2247440 Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5.
  18. 2374930 Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3.
  19. 2404284 Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501.
  20. 2419329 Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51.
  21. 2437111 Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73.
  22. 2727704 Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8.
  23. 2762316 Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6.
  24. 2911589 Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8.
  25. 3009475 Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57.
  26. 3087352 Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8.
  27. 3474609 Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7.
  28. 3479777 Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5.
  29. 3828358 Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7.
  30. 6171778 Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114.
  31. 6275391 Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5.
  32. 656055 Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9.
  33. 7852505 Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7.
  34. 7895732 Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65.
  35. 7902134 Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32.
  36. 8022807 Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80.
  37. 8048949 Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7.
  38. 8347685 Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50.
  39. 8513793 Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44.
  40. 9329347 Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50.
  41. 955075 Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5.
  42. 9589637 Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54.
  43. 9731778 Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35.
Target 1 Drug References
  1. Sloand EM, Klein HG, Pastakia KB, Pierce P, Prodouz KN: Effect of albumin on the inhibition of platelet aggregation by beta-lactam antibiotics. Blood. 1992 Apr 15;79(8):2022-7. [PubMed Link Image]
  2. Markovich MN, Aver'eva EV: [Microcalorimetry study of pharmacological complexes. The binding of cephalosporins with human serum albumin] Antibiot Med Biotekhnol. 1985 Dec;30(12):916-8. [PubMed Link Image]
  3. Decroix MO, Chaumeil JC, Flouvat B: Binding of cefalotin to human serum albumin. Eur J Drug Metab Pharmacokinet. 1984 Jul-Sep;9(3):191-4. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 633
Target 2 Name Penicillin-binding proteins 1A/1B
Target 2 Synonyms Not Available
Target 2 Gene Name pbpA
Target 2 Protein Sequence >Penicillin-binding proteins 1A/1B
MTERKREHKDRKQNKNSPKNQSKVTKFLKWFFIGILLLGITAVTVVGIYVLSIIRSSPEL
DVQAIQSLNQPSILYDDQGNFMDNVITREQRYVVKSEEIPDNLKKAFVAIEDERFYEHKG
IDIKRIFGVIASNIKGKLSGSNTVQGASTITQQLIKNAVLTNEVSYERKIKEMYLALELE
KHLSKDEILTTYLNTIPMGGYQYGVSAAAQRFFSKNVSDLNLVECAYLGGLTQAPTSYDG
LSEANKENPSRYLNRTKSVLFKMHELGYISSEQYNDAINEIDTNGIKFTPNNKLSKTNFE
WFTRPAITQVKQDLMDKYKYTQEEVDKLIANGGLKIYTSMDRNLQNNVQKVLDDPNNYKA
ITNNPNEKNEDGVYKLQASATIIDYKTGHVKALVGGRGEQPAMSHNRAYYDLKSIGSATK
PLTVYGPAIDLGLGGAGSVVNDSPLSNKELSSTGYKDQPKNEYNSYRGPLTFREAIKISS
NLAAIKVANEVGVSNSIAYGEKLGLVYGPHSRGISTTALGQFQNDPNNPDGGNTYTLASA
FGVFGNNGVKTNAKLYTKVLDSHGNVILDTSTPEETKIFSPQASYIVYDMLKDQVESGSA
KSAKFGNIPVAGKTGTTTGDKDYLFAGLTPYYSAAIWIGYDKPREMRTSSGTVTSPIFGK
IMGLAHKDLQYKEVDNLVE
Target 2 Number of Residues 690
Target 2 Molecular Weight 75178
Target 2 Theoretical pI 9.09
Target 2 GO Classification
Function
binding
drug binding
penicillin binding
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
hydrolase activity
peptidase activity
catalytic activity
Process
cellular physiological process
cell organization and biogenesis
external encapsulating structure organization and biogenesis
cell wall organization and biogenesis
cell wall organization and biogenesis (sensu Bacteria)
cell wall biosynthesis (sensu Bacteria)
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
cellular carbohydrate metabolism
peptidoglycan metabolism
peptidoglycan biosynthesis
Component
cell
external encapsulating structure
cell wall
cell wall (sensu Bacteria)
Target 2 General Function Cell wall/membrane/envelope biogenesis
Target 2 Specific Function Not Available
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 30-52
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 18145626 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q8XJ01 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name Q8XJ01_CLOPE Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >2040 bp
ATGACTGAAAGAAAAAGAGAGCATAAAGATAGAAAGCAGAATAAAAATTCACCTAAAAAT
CAATCGAAAGTAACAAAATTTTTGAAATGGTTCTTTATAGGGATTCTGCTTCTAGGGATA
ACTGCCGTAACAGTAGTTGGAATTTACGTTCTTTCTATTATACGTTCATCTCCAGAGTTA
GATGTTCAGGCAATTCAATCTCTAAATCAGCCATCCATTCTTTACGATGATCAGGGAAAC
TTTATGGATAATGTTATAACTCGTGAACAACGTTATGTAGTTAAATCTGAAGAGATACCT
GATAACTTAAAAAAGGCTTTTGTAGCTATTGAAGACGAAAGATTTTATGAGCATAAAGGA
ATAGACATTAAAAGAATTTTTGGGGTAATAGCTTCTAATATTAAAGGTAAACTTTCAGGA
AGTAATACAGTTCAAGGGGCTTCAACCATAACTCAGCAACTTATAAAAAATGCCGTACTT
ACTAATGAAGTTAGTTATGAAAGAAAAATTAAAGAAATGTACTTAGCTTTGGAATTAGAA
AAGCACCTTTCAAAAGATGAAATCCTTACTACGTATTTAAATACAATTCCTATGGGTGGA
TACCAATATGGGGTTAGCGCAGCTGCTCAAAGATTTTTTAGTAAGAATGTTTCAGATTTG
AATTTAGTTGAGTGCGCTTATTTAGGAGGACTTACTCAAGCACCAACTTCTTATGATGGT
CTTTCAGAAGCAAATAAAGAAAATCCAAGTAGATATTTAAATAGAACTAAATCTGTACTA
TTTAAAATGCATGAACTTGGATATATTTCAAGTGAACAATATAATGACGCAATAAATGAA
ATTGACACAAATGGTATAAAATTCACACCAAATAATAAATTAAGTAAAACTAACTTTGAG
TGGTTCACAAGACCAGCTATAACTCAAGTTAAACAAGACTTAATGGATAAATATAAATAT
ACACAAGAGGAAGTTGACAAACTTATAGCTAATGGTGGATTAAAAATCTATACTTCAATG
GATAGAAATCTTCAAAATAATGTTCAAAAAGTTTTAGATGATCCAAATAACTATAAAGCT
ATAACTAATAATCCTAATGAAAAAAATGAAGATGGTGTTTATAAATTACAAGCATCTGCC
ACAATAATAGACTATAAAACAGGCCATGTTAAGGCTTTAGTTGGAGGAAGAGGGGAACAA
CCTGCTATGTCTCACAATAGAGCTTATTATGATTTAAAATCTATAGGTTCTGCAACAAAA
CCATTAACAGTTTATGGTCCTGCTATTGATTTAGGACTTGGTGGCGCTGGCTCTGTAGTA
AATGATTCTCCATTAAGTAATAAAGAGTTATCTTCTACAGGATATAAAGATCAACCTAAG
AATGAATACAATAGTTATAGAGGCCCTTTAACTTTTAGAGAAGCAATTAAAATCTCTAGT
AACTTAGCAGCCATAAAAGTTGCTAATGAAGTAGGTGTTTCAAACTCTATAGCTTATGGA
GAAAAATTAGGTCTTGTTTATGGACCTCATTCTAGAGGTATTTCCACAACAGCCTTAGGT
CAATTCCAAAATGACCCTAATAATCCTGATGGAGGAAATACTTATACTCTAGCTTCAGCC
TTCGGTGTTTTTGGTAATAACGGTGTTAAAACAAATGCTAAATTATATACAAAGGTATTA
GATTCTCATGGAAATGTAATTCTTGATACAAGTACTCCAGAAGAAACTAAAATATTTAGT
CCTCAAGCGTCTTATATAGTTTATGATATGCTTAAGGATCAAGTAGAAAGTGGCTCTGCA
AAATCTGCTAAATTTGGTAATATTCCTGTGGCGGGTAAAACAGGAACTACTACTGGAGAT
AAAGACTATTTATTTGCAGGATTAACTCCATATTATTCTGCGGCTATTTGGATTGGATAT
GATAAGCCTAGAGAAATGAGAACTAGTAGTGGTACTGTTACCTCTCCTATTTTCGGAAAA
ATAATGGGCTTAGCTCATAAAGACTTACAGTACAAAGAGGTTGACAACCTAGTGGAATAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  3. Botta GA, Buffa D: Murein synthesis and beta-lactam antibiotic susceptibility during rod-to-sphere transition in a pbpA(Ts) mutant of Escherichia coli. Antimicrob Agents Chemother. 1981 May;19(5):891-900. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1976
Target 3 Name Endosialin
Target 3 Synonyms
  1. CD248 antigen
  2. Endosialin precursor
  3. Tumor endothelial marker 1
Target 3 Gene Name CD248
Target 3 Protein Sequence >Endosialin precursor
MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDLAT
PRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTNWAQP
ASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALQDEAGQAGPAVYT
TPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNG
GCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGF
RPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQA
SQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREP
QIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDH
QIPVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAG
TQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPV
SPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLALWLP
SPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGPHAPNK
RITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV
Target 3 Number of Residues 769
Target 3 Molecular Weight 80860
Target 3 Theoretical pI 5.03
Target 3 GO Classification
Function
carbohydrate binding
sugar binding
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 3 General Function Involved in calcium ion binding
Target 3 Specific Function May play a role in tumor angiogenesis
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-17
Target 3 Transmembrane Regions
  • 688-708
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 9857400 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q9HCU0 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name CD248_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Membrane
  • single-pass type I membrane protein (Probable)
Target 3 Gene Sequence >2274 bp
ATGCTGCTGCGCCTGTTGCTGGCCTGGGCGGCCGCAGGGCCCACACTGGGCCAGGACCCC
TGGGCTGCTGAGCCCCGTGCCGCCTGCGGCCCCAGCAGCTGCTACGCTCTCTTCCCACGG
CGCCGCACCTTCCTGGAGGCCTGGCGGGCCTGCCGCGAGCTGGGGGGCGACCTGGCCACT
CCTCGGACCCCCGAGGAGGCCCAGCGTGTGGACAGCCTGGTGGGTGCGGGCCCAGCCAGC
CGGCTGCTGTGGATCGGGCTGCAGCGGCAGGCCCGGCAATGCCAGCTGCAGCGCCCACTG
CGCGGCTTCACGTGGACCACAGGGGACCAGGACACGGCTTTCACCAACTGGGCCCAGCCA
GCCTCTGGAGGCCCCTGCCCGGCCCAGCGCTGTGTGGCCCTGGAGGCAAGTGGCGAGCAC
CGCTGGCTGGAGGGCTCGTGCACGCTGGCTGTCGACGGCTACCTGTGCCAGTTTGGCTTC
GAGGGCGCCTGCCCGGCGCTGCAAGATGAGGCGGGCCAGGCCGGCCCAGCCGTGTATACC
ACGCCCTTCCACCTGGTCTCCACAGAGTTTGAGTGGCTGCCCTTCGGCTCTGTGGCCGCT
GTGCAGTGCCAGGCTGGCAGGGGAGCCTCTCTGCTCTGCGTGAAGCAGCCTGAGGGAGGT
GTGGGCTGGTCACGGGCTGGGCCCCTGTGCCTGGGGACTGGCTGCAGCCCTGACAACGGG
GGCTGCGAACACGAATGTGTGGAGGAGGTGGATGGTCACGTGTCCTGCCGCTGCACTGAG
GGCTTCCGGCTGGCAGCAGACGGGCGCAGTTGCGAGGACCCCTGTGCCCAGGCTCCGTGC
GAGCAGCAGTGTGAGCCCGGTGGGCCACAAGGCTACAGCTGCCACTGTCGCCTGGGTTTC
CGGCCAGCGGAGGATGATCCGCACCGCTGTGTGGACACAGATGAGTGCCAGATTGCCGGT
GTGTGCCAGCAGATGTGTGTCAACTACGTTGGTGGCTTCGAGTGTTATTGTAGCGAGGGA
CATGAGCTGGAGGCTGATGGCATCAGCTGCAGCCCTGCAGGGGCCATGGGTGCCCAGGCT
TCCCAGGACCTCGGAGATGAGTTGCTGGATGACGGGGAGGATGAGGAAGATGAAGACGAG
GCCTGGAAGGCCTTCAACGGTGGCTGGACGGAGATGCCTGGGATCCTGTGGATGGAGCCT
ACGCAGCCGCCTGACTTTGCCCTGGCCTATAGACCGAGCTTCCCAGAGGACAGAGAGCCA
CAGATACCCTACCCGGAGCCCACCTGGCCACCCCCGCTCAGTGCCCCCAGGGTCCCCTAC
CACTCCTCAGTGCTCTCCGTCACCCGGCCTGTGGTGGTCTCTGCCACGCATCCCACACTG
CCTTCTGCCCACCAGCCTCCTGTGATCCCTGCCACACACCCAGCTTTGTCCCGTGACCAC
CAGATCCCCGTGATCGCAGCCAACTATCCAGATCTGCCTTCTGCCTACCAACCCGGTATT
CTCTCTGTCTCTCATTCAGCACAGCCTCCTGCCCACCAGCCCCCTATGATCTCAACCAAA
TATCCGGAGCTCTTCCCTGCCCACCAGTCCCCCATGTTTCCAGACACCCGGGTCGCTGGC
ACCCAGACCACCACTCATTTGCCTGGAATCCCACCTAACCATGCCCCTCTGGTCACCACC
CTCGGTGCCCAGCTACCCCCTCAAGCCCCAGATGCCCTTGTCCTCAGAACCCAGGCCACC
CAGCTTCCCATTATCCCAACTGCCCAGCCCTCTCTGACCACCACCTCCAGGTCCCCTGTG
TCTCCTGCCCATCAAATCTCTGTGCCTGCTGCCACCCAGCCCGCAGCCCTCCCCACCCTC
CTGCCCTCTCAGAGCCCCACTAACCAGACCTCACCCATCAGCCCTACACATCCCCATTCC
AAAGCCCCCCAAATCCCAAGGGAAGATGGCCCCAGTCCCAAGTTGGCCCTGTGGCTGCCC
TCACCAGCTCCCACAGCAGCCCCAACAGCCCTGGGGGAGGCTGGTCTTGCCGAGCACAGC
CAGAGGGATGACCGGTGGCTGCTGGTGGCACTCCTGGTGCCAACGTGTGTCTTTTTGGTG
GTCCTGCTTGCACTGGGCATCGTGTACTGCACCCGCTGTGGCCCCCATGCACCCAACAAG
CGCATCACTGACTGCTATCGCTGGGTCATCCATGCTGGGAGCAAGAGCCCAACAGAACCC
ATGCCCCCCAGGGGCAGCCTCACAGGGGTGCAGACCTGCAGAACCAGCGTGTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID CD248 Link Image
Target 3 GenAtlas ID CD248 Link Image
Target 3 HGNC ID HGNC:18219 Link Image
Target 3 Chromosome Location 11
Target 3 Locus 11q13
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. St Croix B, Rago C, Velculescu V, Traverso G, Romans KE, Montgomery E, Lal A, Riggins GJ, Lengauer C, Vogelstein B, Kinzler KW: Genes expressed in human tumor endothelium. Science. 2000 Aug 18;289(5482):1197-202. [PubMed Link Image]
  2. Christian S, Ahorn H, Koehler A, Eisenhaber F, Rodi HP, Garin-Chesa P, Park JE, Rettig WJ, Lenter MC: Molecular cloning and characterization of endosialin, a C-type lectin-like cell surface receptor of tumor endothelium. J Biol Chem. 2001 Mar 9;276(10):7408-14. Epub 2000 Nov 17. [PubMed Link Image]
Target 3 Drug References
  1. Diaz N, Suarez D, Merz KM Jr, Sordo TL: Molecular dynamics simulations of the TEM-1 beta-lactamase complexed with cephalothin. J Med Chem. 2005 Feb 10;48(3):780-91. [PubMed Link Image]
  2. Petit A, Ben Yaghlane-Bouslama H, Sofer L, Labia R: Does high level production of SHV-type penicillinase confer resistance to ceftazidime in Enterobacteriaceae? FEMS Microbiol Lett. 1992 Apr 1;71(1):89-94. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 2461
Target 4 Name D-alanyl-D-alanine carboxypeptidase
Target 4 Synonyms
  1. D-alanyl-D-alanine carboxypeptidase precursor
  2. DD- peptidase
  3. DD-carboxypeptidase
  4. EC 3.4.16.4
Target 4 Gene Name Not Available
Target 4 Protein Sequence >D-alanyl-D-alanine carboxypeptidase precursor
MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVR
VDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNT
YLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGV
TNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTH
ANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQ
QWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNV
NVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD
Target 4 Number of Residues 412
Target 4 Molecular Weight 42917
Target 4 Theoretical pI 6.03
Target 4 GO Classification
Function
Not Available
Process
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
Component
Not Available
Target 4 General Function Involved in cell wall peptidoglycan synthesis
Target 4 Specific Function Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e., a D-alanyl-D-alanine- terminated peptide), it becomes immobilized in the form of a long- lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP)
Target 4 Pathways Not Available
Target 4 Reactions
  • Preferential cleavage: (Ac)2-L-Lys-D-Ala!D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine INHIBITOR Penicillin; beta-Lactam antibiotics
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-31
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 515050 Link Image
Target 4 UniProtKB/Swiss-Prot ID P15555 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name DAC_STRSR Link Image
Target 4 PDB ID 1PWG Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Secreted protein
Target 4 Gene Sequence >1221 bp
ATGGTCTCAGGAACGGTGGGCAGAGGTACGGCGCTGGGCGCGGTGCTGTTGGCCCTCCTC
GCAGTCCCCGCACAGGCCGGCACCGCCGCGGCCGCGGATCTGCCGGCACCCGACGACACC
GGTCTGCAGGCGGTGCTGCACACGGCCCTTTCCCAGGGAGCCCCCGGTGCGATGGTGCGG
GTCGACGACAACGGCACGATCCACCAGTTGTCGGAGGGAGTCGCCGACCGGGCCACCGGG
CGTGCGATCACCACGACCGACCGGTTCCGCGTCGGCAGCGTCACCAAGAGCTTCTCCGCC
GTGGTCCTGCTGCAACTGGTGGACGAGGGCAAGCTCGACCTGGACGCTTCGGTGAACACC
TATCTGCCCGGGCTGCTGCCCGACGACCGGATCACCGTGCGTCAGGTGATGAGCCACCGC
AGTGGGCTGTACGACTACACCAACGACATGTTCGCGCAGACGGTCCCGGGCTTCGAGTCC
GTCCGCAACAAGGTCTTCAGCTACCAGGACCTGATCACCCTGTCCCTCAAGCACGGGGTC
ACCAACGCACCGGGCGCGGCCTATTCATACTCCAACACGAACTTCGTCGTCGCGGGCATG
CTCATCGAGAAGCTCACCGGCCACTCCGTGGCCACGGAGTACCAGAACCGCATCTTCACG
CCGCTGAACCTGACCGACACCTTCTACGTGCACCCCGACACCGTCATCCCGGGCACCCAC
GCCAACGGCTACCTCACGCCGGACGAGGCCGGTGGGGCCCTGGTCGACTCCACCGAGCAG
ACGGTGTCGTGGGCGCAGAGCGCGGGCGCGGTCATCTCCAGCACGCAGGACCTGGACACG
TTCTTCTCCGCGTTGATGAGCGGGCAGCTCATGTCCGCCGCGCAGCTCGCGCAGATGCAG
CAGTGGACGACGGTCAACAGCACCCAGGGGTACGGCCTCGGCCTGCGCCGCCGTGACCTG
TCCTGCGGTATCTCGGTGTACGGCCACACGGGCACCGTGCAGGGCTACTACACGTACGCC
TTCGCCTCGAAGGACGGCAAGCGCAGCGTCACCGCGCTCGCCAACACCTCGAACAACGTG
AACGTGCTGAACACGATGGCCCGCACGCTGGAATCCGCGTTCTGCGGCAAGCCGACGACC
GCGAAGCTGCGCAGCGCGACCTCCTCGGCGACCACCGTGGAGCGCCACGAGGACATCGCG
CCGGGTATCGCCCGCGACTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs Not Available
Target 4 General References
  1. Piron-Fraipont C, Lenzini MV, Dusart J, Ghuysen JM: Transcriptional analysis of the DD-peptidase/penicillin-binding protein-encoding dac gene of Streptomyces R61: use of the promoter and signal sequences in a secretion vector. Mol Gen Genet. 1990 Aug;223(1):114-20. [PubMed Link Image]
  2. Knox JR, Pratt RF: Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein. Antimicrob Agents Chemother. 1990 Jul;34(7):1342-7. [PubMed Link Image]
  3. Joris B, Jacques P, Frere JM, Ghuysen JM, Van Beeumen J: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data. Eur J Biochem. 1987 Feb 2;162(3):519-24. [PubMed Link Image]
  4. Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1987 Feb 2;162(3):509-18. [PubMed Link Image]
  5. Kelly JA, Knox JR, Moews PC, Hite GJ, Bartolone JB, Zhao H, Joris B, Frere JM, Ghuysen JM: 2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams. J Biol Chem. 1985 May 25;260(10):6449-58. [PubMed Link Image]
  6. Kelly JA, Kuzin AP: The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution. J Mol Biol. 1995 Nov 24;254(2):223-36. [PubMed Link Image]
  7. Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1994 Sep 15;224(3):1079. [PubMed Link Image]
Target 4 Drug References
  1. Frere JM, Geurts F, Ghuysen JM: The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G. Interaction with beta-lactam antibiotics. Biochem J. 1978 Dec 1;175(3):801-5. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. Wrezel PW, Ellis LF, Neuhaus FC: In vivo target of benzylpenicillin in Gaffkya homari. Antimicrob Agents Chemother. 1986 Mar;29(3):432-9. [PubMed Link Image]
  5. Kuzin AP, Liu H, Kelly JA, Knox JR: Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Biochemistry. 1995 Jul 25;34(29):9532-40. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 2478
Target 5 Name Beta-lactamase
Target 5 Synonyms
  1. Beta-lactamase precursor
  2. Cephalosporinase
  3. EC 3.5.2.6
Target 5 Gene Name ampC
Target 5 Protein Sequence >Beta-lactamase precursor
MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG
YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI
TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK
PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK
STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII
NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY
PNPARVDAAWQILNALQ
Target 5 Number of Residues 383
Target 5 Molecular Weight 41556
Target 5 Theoretical pI 9.07
Target 5 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
beta-lactamase activity
Process
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
physiological process
metabolism
cellular metabolism
drug metabolism
antibiotic metabolism
antibiotic catabolism
Component
cell
periplasmic space
periplasmic space (sensu Gram-negative Bacteria)
Target 5 General Function Defense mechanisms and antibiotic degradation
Target 5 Specific Function This protein is a serine beta-lactamase with a substrate specificity for cephalosporins
Target 5 Pathways
Name SMPDB Link KEGG Link
Penicillins and cephalosporins biosynthesis map00311 Link Image
Target 5 Reactions
  • a beta-lactam + H2O = a substituted beta-amino acid
Target 5 Pfam Domain Function
Target 5 Signals
  • 1-19
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Essential
Target 5 GenBank ID Protein 145267 Link Image
Target 5 UniProtKB/Swiss-Prot ID P00811 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name AMPC_ECOLI Link Image
Target 5 PDB ID 1XGJ Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Periplasm
Target 5 Gene Sequence >1134 bp
ATGTTCAAAACGACGCTCTGCGCCTTATTAATTACCGCCTCTTGCTCCACATTTGCTGCC
CCTCAACAAATCAACGATATTGTGCATCGCACAATTACCCCGCTTATAGAGCAACAAAAG
ATCCCGGGTATGGCGGTGGCGGTAATTTATCAGGGTAAACCTTATTACTTTACCTGGGGC
TATGCGGACATCGCCAAAAAGCAGCCCGTCACACAGCAAACGTTGTTTGAGTTAGGTTCG
GTCAGCAAAACATTTACTGGCGTGCTTGGTGGCGACGCTATTGCTCGAGGGGAAATCAAG
TTAAGCGATCCCACAACAAAATACTGGCCTGAACTTACCGCTAAACAGTGGAATGGGATC
ACACTATTACATCTCGCAACCTACACTGCTGGCGGCCTGCCATTGCAGGTGCCGGATGAG
GTGAAATCCTCAAGCGACTTGCTGCGCTTCTATCAAAACTGGCAGCCTGCATGGGCTCCA
GGAACACAACGTCTGTATGCCAACTCCAGTATCGGTTTGTTCGGCGCACTGGCTGTGAAG
CCGTCTGGTTTGAGTTTTGAGCAGGCGATGCAAACTCGTGTCTTCCAGCCACTCAAACTC
AACCATACGTGGATTAATGTACCGCCCGCAGAAGAAAAGAATTACGCCTGGGGATATCGC
GAAGGTAAGGCAGTGCATGTTTCGCCTGGGGCGTTAGATGCTGAAGCTTATGGTGTGAAG
TCGACCATTGAAGATATGGCCCGCTGGGTGCAAAGCAATTTAAAACCCCTTGATATCAAT
GAGAAAACGCTTCAACAAGGGATACAACTGGCACAATCTCGCTACTGGCAAACCGGCGAT
ATGTATCAGGGCCTGGGCTGGGAAATGCTGGACTGGCCGGTAAATCCTGACAGCATCATT
AACGGCAGTGACAATAAAATTGCACTGGCAGCACGCCCCGTAAAAGCGATTACGCCCCCA
ACTCCTGCAGTACGCGCATCATGGGTACATAAAACAGGGGCGACCGGCGGATTTGGTAGC
TATGTCGCGTTTATTCCAGAAAAAGAGCTGGGTATCGTGATGCTGGCAAACAAAAACTAT
CCCAATCCAGCGAGAGTCGACGCCGCCTGGCAGATTCTTAACGCTCTACAGTAA
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus Not Available
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Powers RA, Blazquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK: The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase. Protein Sci. 1999 Nov;8(11):2330-7. [PubMed Link Image]
  2. Powers RA, Caselli E, Focia PJ, Prati F, Shoichet BK: Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design. Biochemistry. 2001 Aug 7;40(31):9207-14. [PubMed Link Image]
  3. Beadle BM, Shoichet BK: Structural bases of stability-function tradeoffs in enzymes. J Mol Biol. 2002 Aug 9;321(2):285-96. [PubMed Link Image]
  4. Morandi F, Caselli E, Morandi S, Focia PJ, Blazquez J, Shoichet BK, Prati F: Nanomolar inhibitors of AmpC beta-lactamase. J Am Chem Soc. 2003 Jan 22;125(3):685-95. [PubMed Link Image]
  5. Jaurin B, Grundstrom T: ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897-901. [PubMed Link Image]
  6. Grundstrom T, Jaurin B: Overlap between ampC and frd operons on the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1111-5. [PubMed Link Image]
  7. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  8. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  9. Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ: Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design. Biochemistry. 1998 Nov 17;37(46):16082-92. [PubMed Link Image]
Target 5 Drug References
  1. Diaz N, Suarez D, Merz KM Jr, Sordo TL: Molecular dynamics simulations of the TEM-1 beta-lactamase complexed with cephalothin. J Med Chem. 2005 Feb 10;48(3):780-91. [PubMed Link Image]
  2. Oelschlaeger P, Mayo SL, Pleiss J: Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci. 2005 Mar;14(3):765-74. [PubMed Link Image]
  3. Bethel CR, Hujer AM, Hujer KM, Thomson JM, Ruszczycky MW, Anderson VE, Pusztai-Carey M, Taracila M, Helfand MS, Bonomo RA: Role of Asp104 in the SHV beta-lactamase. Antimicrob Agents Chemother. 2006 Dec;50(12):4124-31. Epub 2006 Sep 18. [PubMed Link Image]
  4. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  5. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.