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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-05-01 18:16:07
Primary Accession Number DB00560
Secondary Accession Number
  • APRD01307
Name Tigecycline
Drug Type
  • Small Molecule
Description Tigecycline is a glycylcycline antibiotic developed and marketed by Wyeth under the brand name Tygacil. It was given a U.S. Food and Drug Administration (FDA) fast-track approval and was approved on June 17, 2005. It was developed in response to the growing prevalence of antibiotic resistance in bacteria such as Staphylococcus aureus.
Synonyms
  1. GAR-936
  2. GAR-936,Tigecycline
  3. WAY-GAR-936
Brand Names
  1. Tygacil
Brand Mixtures Not Available
Chemical IUPAC Name N-[(5aR,6aS,7S,9Z,10aS)-9-(amino-hydroxymethylidene)-4,7-bis(dimethylamino)-1,10a,12-trihydroxy-8,10,11-trioxo-5a,6,6a,7-tetrahydro-5H-tetracen-2-yl]-2-(tert-butylamino)acetamide
Chemical Formula C29H39N5O8
Chemical Structure Structure
CAS Registry Number 220620-09-7
InChI Identifier InChI=1/C29H39N5O8/c1-28(2,3)31-11-17(35)32-15-10-16(33(4)5)13-8-12-9-14-21(34(6)7)24(38)20(27(30)41)26(40)29(14,42)25(39)18(12)23(37)19(13)22(15)36/h10,12,14,21,31,36-37,41-42H,8-9,11,30H2,1-7H3,(H,32,35)/b27-20-/t12-,14-,21-,29-/m0/s1/f/h32H
InChI Key ZXGBRIBPJBHLMO-WCTWHVKXDK
KEGG Drug D01079 Link Image
KEGG Compound C12012 Link Image
PubChem Compound 5282044 Link Image
PubChem Substance 14170 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic4/tygacil.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Tigecycline Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 585.6487
Monoisotopic Molecular Weight 585.2799
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.51e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.8 Source: PhysProp
Predicted LogP 0.81 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.11 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 Not Available
Isomeric SMILES CN(C)[C@H]1[C@@H]2C[C@@H]3CC4=C(C=C(NC(=O)CNC(C)(C)C)C(O)=C4C(O)=C3C(=O)[C@]2(O)C(=O)\C(C1=O)=C(\N)O)N(C)C
Canonical SMILES CN(C)C1C2CC3CC4=C(C=C(NC(=O)CNC(C)(C)C)C(O)=C4C(O)=C3C(=O)C2(O)C(=O)C(C1=O)=C(N)O)N(C)C
Drug Category
  • Anti-Bacterial Agents
  • Antibacterial Agents
  • Tetracyclines
ATC Codes
AHFS Codes
  • 08:12.24
Indication For the treatment of infections caused by susceptible strains of the designated microorganisms in the following conditions: Complicated skin and skin structure infections caused by Escherichia coli, Enterococcus faecalis (vancomycin-susceptible isolates only), Staphylococcus aureus (methicillin-susceptible and -resistant isolates), Streptococcus agalactiae, Streptococcus anginosus grp. (includes S. anginosus, S. intermedius, and S. constellatus), Streptococcus pyogenes and Bacteroides fragilis. Complicated intra-abdominal infections caused by Citrobacter freundii, Enterobacter cloacae, Escherichia coli, Klebsiella oxytoca, Klebsiella pneumoniae, Enterococcus faecalis (vancomycin-susceptible isolates only), Staphylococcus aureus (methicillin-susceptible isolates only), Streptococcus anginosus grp. (includes S. anginosus, S. intermedius, and S. constellatus), Bacteroides fragilis, Bacteroides thetaiotaomicron, Bacteroides uniformis, Bacteroides vulgatus, Clostridium perfringens, and Peptostreptococcus micros.
Pharmacology Tigecycline is the first clinically-available drug in a new class of antibiotics called the glycylcyclines. Glycylcyclines are a new class of antibiotics derived from tetracycline. These tetracycline analogues are specifically designed to overcome two common mechanisms of tetracycline resistance, namely resistance mediated by acquired efflux pumps and/or ribosomal protection. Glycylcycline antibiotics have a similar mechanism of action as tetracycline antibiotics. Both classes of antibiotics bind to the 30S ribosomal subunit to prevent the amino-acyl tRNA from binding to the A site of the ribosome. However, the glycylcyclines appear to bind more effectively than the tetracyclines.
Mechanism of Action Tigecycline, a glycylcycline, inhibits protein translation in bacteria by binding to the 30S ribosomal subunit and blocking entry of amino-acyl tRNA molecules into the A site of the ribosome. This prevents incorporation of amino acid residues into elongating peptide chains. Tigecycline carries a glycylamido moiety attached to the 9-position of minocycline. The substitution pattern is not present in any naturally occurring or semisynthetic tetracycline and imparts certain microbiologic properties to tigecycline. Tigecycline is not affected by the two major tetracycline resistance mechanisms, ribosomal protection and efflux. Accordingly, tigecycline has demonstrated in vitro and in vivo activity against a broad spectrum of bacterial pathogens. There has been no cross resistance observed between tigecycline and other antibiotics. Tigecycline is not affected by resistance mechanisms such as beta-lactamases (including extended spectrum beta-lactamases), target site modifications, macrolide efflux pumps or enzyme target changes (e.g. gyrase/topoisomerase). In vitro studies have not demonstrated antagonism between tigecycline and other commonly used antibacterial drugs. In general, tigecycline is considered bacteriostatic.
Absorption Not Available
Toxicity Since glycylcyclines are similar to tetracyclines, they share many of the same side effects and contraindications as tetracyclines. These side effects may include nausea/vomiting, headache, photosensitivity, discoloration of growing teeth, and fetal damage.
Protein Binding 71% to 89%
Biotransformation Tigecycline is not extensively metabolized. In vitro studies with tigecycline using human liver microsomes, liver slices, and hepatocytes led to the formation of only trace amounts of metabolites. A glucuronide, an N-acetyl metabolite, and a tigecycline epimer (each at no more than 10% of the administered dose) are the primary metabolites.
Half Life 27-43 hours
Dosage Forms
Form Route
Powder, for solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol Tigecycline increases the anticoagulant effect
Anisindione Tigecycline increases the anticoagulant effect
Dicumarol Tigecycline increases the anticoagulant effect
Warfarin Tigecycline increases the anticoagulant effect
Food Interactions Not Available
Pathways Not Available
General References
  1. Kasbekar N: Tigecycline: a new glycylcycline antimicrobial agent. Am J Health Syst Pharm. 2006 Jul 1;63(13):1235-43. [PubMed Link Image]
  2. Rose WE, Rybak MJ: Tigecycline: first of a new class of antimicrobial agents. Pharmacotherapy. 2006 Aug;26(8):1099-110. [PubMed Link Image]
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. 30S ribosomal protein S4
  2. 30S ribosomal protein S9
  3. 16S rRNA
Drug Target 1 [top]
Target 1 ID 22
Target 1 Name 30S ribosomal protein S4
Target 1 Synonyms Not Available
Target 1 Gene Name rpsD
Target 1 Protein Sequence >30S ribosomal protein S4 
ARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQKV
RRIYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSHK
AIMVNGRVVNIASYQVSPNDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEGT
FKRKPERSDLSADINEHLIVELYSK
Target 1 Number of Residues 208
Target 1 Molecular Weight 23338
Target 1 Theoretical pI 10.66
Target 1 GO Classification
Function
binding
nucleic acid binding
RNA binding
structural molecule activity
structural constituent of ribosome
Process
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
Component
cell
intracellular
protein complex
ribonucleoprotein complex
ribosome
small ribosomal subunit
Target 1 General Function Translation, ribosomal structure and biogenesis
Target 1 Specific Function Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 42798 Link Image
Target 1 UniProtKB/Swiss-Prot ID P0A7V8 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name RS4_ECOLI Link Image
Target 1 PDB ID 1P87 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >621 bp 
ATGGCAAGATATTTGGGTCCTAAGCTCAAGCTGAGCCGTCGTGAGGGCACCGACTTATTC
CTTAAGTCTGGCGTTCGCGCGATCGATACCAAGTGTAAAATTGAACAAGCTCCTGGCCAG
CACGGTGCGCGTAAACCGCGTCTGTCTGACTATGGTGTGCAGTTGCGTGAAAAGCAAAAA
GTTCGCCGTATCTATGGTGTGCTGGAGCGTCAGTTCCGTAACTACTACAAAGAAGCAGCA
CGTCTGAAAGGCAACACCGGTGAAAACCTGTTGGCTCTGCTGGAAGGTCGTCTGGACAAC
GTTGTATACCGTATGGGCTTCGGTGCCACTCGTGCAGAAGCACGTCAGCTGGTTAGCCAT
AAAGCAATTATGGTAAACGGTCGTGTTGTTAACATCGCTTCTTATCAGGTTAGTCCGAAT
GACGTTGTAAGCATTCGTGAGAAAGCGAAGAAGCAGTCTCGCGTGAAAGCCGCTCTGGAG
CTGGCTGAGCAGCGTGAAAAGCCAACCTGGCTGGAAGTTGATGCTGGCAAGATGGAAGGT
ACGTTTAAGCGTAAGCCGGAGCGTTCTGATCTGTCTGCGGACATTAACGAACACCTGATC
GTCGAGCTTTACTCCAAGTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Arnold RJ, Reilly JP: Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal Biochem. 1999 Apr 10;269(1):105-12. [PubMed Link Image]
  2. Schiltz E, Reinbolt J: Determination of the complete amino-acid sequence of protein S4 from Escherichia coli ribosomes. Eur J Biochem. 1975 Aug 15;56(2):467-81. [PubMed Link Image]
  3. Dahlgren A, Ryden-Aulin M: A novel mutation in ribosomal protein S4 that affects the function of a mutated RF1. Biochimie. 2000 Aug;82(8):683-91. [PubMed Link Image]
  4. Torres M, Condon C, Balada JM, Squires C, Squires CL: Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination. EMBO J. 2001 Jul 16;20(14):3811-20. [PubMed Link Image]
  5. Tung CS, Joseph S, Sanbonmatsu KY: All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol. 2002 Oct;9(10):750-5. [PubMed Link Image]
  6. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J: Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13;113(6):789-801. [PubMed Link Image]
  7. Nowotny V, Nierhaus KH: Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry. 1988 Sep 6;27(18):7051-5. [PubMed Link Image]
  8. Allen PN, Noller HF: Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA. J Mol Biol. 1989 Aug 5;208(3):457-68. [PubMed Link Image]
  9. Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L: Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli. Nucleic Acids Res. 1985 Jun 11;13(11):3891-903. [PubMed Link Image]
  10. Thomas MS, Bedwell DM, Nomura M: Regulation of alpha operon gene expression in Escherichia coli. A novel form of translational coupling. J Mol Biol. 1987 Jul 20;196(2):333-45. [PubMed Link Image]
  11. 387752 Post LE, Nomura M: Nucleotide sequence of the intercistronic region preceding the gene for RNA polymerase subunit alpha in Escherichia coli. J Biol Chem. 1979 Nov 10;254(21):10604-6.
  12. 4587210 Reinbolt J, Schiltz E: The primary structure of ribosomal protein S4 from Escherichia coli. FEBS Lett. 1973 Nov 1;36(3):250-2.
  13. 7556101 Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 1995 Sep 15;14(18):4578-88.
  14. 7559430 Baker AM, Draper DE: Messenger RNA recognition by fragments of ribosomal protein S4. J Biol Chem. 1995 Sep 29;270(39):22939-45.
  15. 9278503 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.
  16. 9716382 Choi KM, Atkins JF, Gesteland RF, Brimacombe R: Flexibility of the nascent polypeptide chain within the ribosome--contacts from the peptide N-terminus to a specific region of the 30S subunit. Eur J Biochem. 1998 Jul 15;255(2):409-13.
Target 1 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]
Drug Target 2 [top]
Target 2 ID 140
Target 2 Name 30S ribosomal protein S9
Target 2 Synonyms Not Available
Target 2 Gene Name rpsI
Target 2 Protein Sequence >30S ribosomal protein S9 
AENQYYGTGRRKSSAARVFIKPGNGKIVINQRSLEQYFGRETARMVVRQPLELVDMVEKL
DLYITVKGGGISGQAGAIRHGITRALMEYDESLRSELRKAGFVTRDARQVERKKVGLRKA
RRRPQFSKR
Target 2 Number of Residues 131
Target 2 Molecular Weight 14725
Target 2 Theoretical pI 11.52
Target 2 GO Classification
Function
structural molecule activity
structural constituent of ribosome
Process
physiological process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
Component
protein complex
ribonucleoprotein complex
ribosome
cell
intracellular
Target 2 General Function Translation, ribosomal structure and biogenesis
Target 2 Specific Function The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 535073 Link Image
Target 2 UniProtKB/Swiss-Prot ID P0A7X3 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name RS9_ECOLI Link Image
Target 2 PDB ID 1P87 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >393 bp 
ATGGCTGAAAATCAATACTACGGCACTGGTCGCCGCAAAAGTTCCGCAGCTCGCGTTTTC
ATCAAACCGGGCAACGGTAAAATCGTAATCAACCAACGTTCTCTGGAACAGTACTTCGGT
CGTGAAACTGCCCGCATGGTAGTTCGTCAGCCGCTGGAACTGGTCGACATGGTTGAGAAA
CTGGACCTGTACATCACCGTTAAAGGTGGTGGTATCTCTGGTCAGGCTGGTGCGATCCGT
CACGGTATCACCCGCGCTCTGATGGAATACGACGAGTCCCTGCGTTCTGAACTGCGTAAA
GCTGGCTTCGTTACTCGTGACGCTCGTCAGGTTGAACGTAAGAAAGTCGGTCTGCGTAAA
GCACGTCGTCGTCCGCAGTTCTCCAAACGTTAA
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. Arnold RJ, Reilly JP: Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal Biochem. 1999 Apr 10;269(1):105-12. [PubMed Link Image]
  2. Chen R, Wittmann-Liebold B: The primary structure of protein S9 from the 30S subunit of Escherichia coli ribosomes. FEBS Lett. 1975 Mar 15;52(1):139-40. [PubMed Link Image]
  3. Tung CS, Joseph S, Sanbonmatsu KY: All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol. 2002 Oct;9(10):750-5. [PubMed Link Image]
  4. Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J: Study of the structural dynamics of the E coli 70S ribosome using real-space refinement. Cell. 2003 Jun 13;113(6):789-801. [PubMed Link Image]
  5. Isono S, Thamm S, Kitakawa M, Isono K: Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli. Mol Gen Genet. 1985;198(2):279-82. [PubMed Link Image]
  6. Marsh RC, Parmeggiani A: Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G. Proc Natl Acad Sci U S A. 1973 Jan;70(1):151-5. [PubMed Link Image]
  7. Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B: Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 1995 Sep 15;14(18):4578-88. [PubMed Link Image]
  8. Osswald M, Doring T, Brimacombe R: The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site. Nucleic Acids Res. 1995 Nov 25;23(22):4635-41. [PubMed Link Image]
  9. 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]
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]
Drug Target 3 [top]
Target 3 ID 883
Target 3 Name 16S rRNA
Target 3 Synonyms
  1. 16S ribosomal ribonucleic acid
Target 3 Gene Name Not Available
Target 3 Protein Sequence Not Available
Target 3 Number of Residues 0
Target 3 Molecular Weight Not Available
Target 3 Theoretical pI Not Available
Target 3 GO Classification
Function
transferase activity
translation
RNA binding
Process
rRNA processing
RNA processing and modification
Component
cell
Target 3 General Function Translation, ribosomal structure and biogenesis
Target 3 Specific Function In prokaryotes, the 16S rRNA is essential for recognizing the 5' end of mRNA and hence positioning it correctly on the ribosome. The 16S rRNA has a characteristic secondary structure in which half of the nucleotides are base-paired. The 16S rRNA sequence has been highly conserved and is often used for evolutionary and species comparative analysis.
Target 3 Pathways
Name SMPDB Link KEGG Link
Ribosome map03010 Link Image
Target 3 Reactions
  • rRNA + mRNA + Amino Acids = Polypeptide
Target 3 Pfam Domain Function Not Available
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein Not Available
Target 3 UniProtKB/Swiss-Prot ID Not Available
Target 3 UniProtKB/Swiss-Prot Entry Name Not Available
Target 3 PDB ID 1EMI Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Cytoplasmic
Target 3 Gene Sequence >16S rRNA sequence 
AAATTGAAGAGTTTGATCATGGCTCAGATTGAACGCTGGCGGCAGGCCTAACACATGCAA
GTCGAACGGTAACAGGAAACAGCTTGCTGTTTCGCTGACGAGTGGCGGACGGGTGAGTAA
TGTCTGGGAAACTGCCTGATGGAGGGGGATAACTACTGGAAACGGTAGCTAATACCGCAT
AACGTCGCAAGACCAAAGAGGGGGACCCTCGGGCCTCTTGCCATCGGATGTGCCCAGATG
GGATTAGCTTGTTGGTGGGGTAACGGCTCACCAAGGCGACGATCCCTAGCTGGTCTGAGA
GGATGACCAGCCACACTGGAACTGAGACACGGTCCAGACTCCTACGGGAGGCAGCAGTGG
GGAATATTGCACAATGGGCGCAAGCCTGATGCAGCCATGCCGCGTGTATGAAGAAGGCCT
TCGGGTTGTAAAGTACTTTCAGCGGGGAGGAAGGGAGTAAAGTTAATACCTTTGCTCATT
GACGTTACCCGCAGAAGAAGCACCGGCTAACTCCGTGCCAGCAGCCGCGGTAATACGGAG
GGTGCAAGCGTTAATCGGAATTACTGGGCGTAAAGCGCACGCAGGCGGTTTGTTAAGTCA
GATGTGAAATCCCCGGGCTCAACCTGGGAACTGCATCTGATACTGGCAAGCTTGAGTCTC
GTAGAGGGGGGTAGAATTCCAGGTGTAGCGGTGAAATGCGTAGAGATCTGGAGGAATACC
GGTGGCGAAGGCGGCCCCCTGGACGAAGACTGACGCTCAGGTGCGAAAGCGTGGGGAGCA
AACAGGATTAGATACCCTGGTAGTCCACGCCGTAAACGATGTCGACTTGGAGGTTGTGCC
CTTGAGGCGTGGCTTCCGGAGCTAACGCGTTAAGTCGACCGCCTGGGGAGTACGGCCGCA
AGGTTAAAACTCAAATGAATTGACGGGGGCCCGCACAAGCGGTGGAGCATGTGGTTTAAT
TCGATGCAACGCGAAGAACCTTACCTGGTCTTGACATCCACGGAAGTTTTCAGAGATGAG
AATGTGCCTTCGGGAACCGTGAGACAGGTGCTGCATGGCTGTCGTCAGCTCGTGTTGTGA
AATGTTGGGTTAAGTCCCGCAACGAGCGCAACCCTTATCCTTTGTTGCCAGCGGTCCGGC
CGGGAACTCAAAGGAGACTGCCAGTGATAAACTGGAGGAAGGTGGGGATGACGTCAAGTC
ATCATGGCCCTTACGACCAGGGCTACACACGTGCTACAATGGCGCATACAAAGAGAAGCG
ACCTCGCGAGAGCAAGCGGACCTCATAAAGTGCGTCGTAGTCCGGATTGGAGTCTGCAAC
TCGACTCCATGAAGTCGGAATCGCTAGTAATCGTGGATCAGAATGCCACGGTGAATACGT
TCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGCAAAAGAAGTAGGT
AGCTTAACCTTCGGGAGGGCGCTTACCACTTTGTGATTCATGACTGGGGTGAAGTCGTAA
CAAGGTAACCGTAGGGGAACCTGCGGTTGGATCACCTCCTTA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs Not Available
Target 3 General References
  1. Gu XR, Gustafsson C, Ku J, Yu M, Santi DV: Identification of the 16S rRNA m5C967 methyltransferase from Escherichia coli. Biochemistry. 1999 Mar 30;38(13):4053-7. [PubMed Link Image]
  2. Martin JF, Barreiro C, Gonzalez-Lavado E, Barriuso M: Ribosomal RNA and ribosomal proteins in corynebacteria. J Biotechnol. 2003 Sep 4;104(1-3):41-53. [PubMed Link Image]
  3. Srivastava AK, Schlessinger D: Structure and organization of ribosomal DNA. Biochimie. 1991 Jun;73(6):631-8. [PubMed Link Image]
  4. Gutell RR, Larsen N, Woese CR: Lessons from an evolving rRNA: 16S and 23S rRNA structures from a comparative perspective. Microbiol Rev. 1994 Mar;58(1):10-26. [PubMed Link Image]
Target 3 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]

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.