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Showing drug card for Chloramphenicol (DB00446)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:11
Primary Accession Number DB00446
Secondary Accession Number
  • APRD00862
  • EXPT00942
Name Chloramphenicol
Drug Type
  • Approved
  • Small Molecule
Description An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106)
Synonyms
  1. CAF
  2. CAM
  3. CAP
  4. CPh
  5. Chloramfenikol
  6. Chloramphenicole
  7. Chloroamphenicol
  8. Cloroamfenicolo
  9. D-Chloramphenicol
Brand Names
  1. Ak-Chlor Ophthalmic Ointment
  2. Ak-Chlor Ophthalmic Solution
  3. Ak-chlor
  4. Alficetyn
  5. Ambofen
  6. Amphenicol
  7. Amphicol
  8. Amseclor
  9. Anacetin
  10. Aquamycetin
  11. Austracil
  12. Austracol
  13. Biocetin
  14. Biophenicol
  15. Catilan
  16. Chemicetin
  17. Chemicetina
  18. Chlomin
  19. Chlomycol
  20. Chlora-Tabs
  21. Chloracol Ophthalmic Solution
  22. Chloramex
  23. Chloramficin
  24. Chloramfilin
  25. Chloramsaar
  26. Chlorasol
  27. Chloricol
  28. Chlornitromycin
  29. Chloro-25 vetag
  30. Chlorocaps
  31. Chlorocid
  32. Chlorocid S
  33. Chlorocide
  34. Chlorocidin C
  35. Chlorocidin C tetran
  36. Chlorocol
  37. Chlorofair
  38. Chlorofair Ophthalmic Ointment
  39. Chlorofair Ophthalmic Solution
  40. Chloroject L
  41. Chloromax
  42. Chloromycetin Hydrocortisone
  43. Chloromycetin Ophthalmic Ointment
  44. Chloromycetin Palmitate
  45. Chloromycetin for Ophthalmic Solution
  46. Chloromycetny
  47. Chloromyxin
  48. Chloronitrin
  49. Chloroptic
  50. Chloroptic Ophthalmic Solution
  51. Chloroptic S.O.P.
  52. Chloroptic-P S.O.P.
  53. Chlorovules
  54. Cidocetine
  55. Ciplamycetin
  56. Cloramfen
  57. Cloramficin
  58. Cloramicol
  59. Cloramidina
  60. Clorocyn
  61. Cloromisan
  62. Clorosintex
  63. Comycetin
  64. Cylphenicol
  65. Desphen
  66. Detreomycin
  67. Detreomycine
  68. Dextromycetin
  69. Doctamicina
  70. Econochlor
  71. Econochlor Ophthalmic Ointment
  72. Econochlor Ophthalmic Solution
  73. Elase-Chloromycetin
  74. Embacetin
  75. Emetren
  76. Enicol
  77. Enteromycetin
  78. Erbaplast
  79. Ertilen
  80. Farmicetina
  81. Farmitcetina
  82. Fenicol
  83. Fenicol Ophthalmic Ointment
  84. Globenicol
  85. Glorous
  86. Halomycetin
  87. Hortfenicol
  88. I-Chlor Ophthalmic Solution
  89. Intramycetin
  90. Isicetin
  91. Ismicetina
  92. Isophenicol
  93. Isopto fenicol
  94. Juvamycetin
  95. Kamaver
  96. Kemicetina
  97. Kemicetine
  98. Klorita
  99. Klorocid S
  100. Leukamycin
  101. Leukomyan
  102. Leukomycin
  103. Levomicetina
  104. Levomitsetin
  105. Levomycetin
  106. Loromisan
  107. Loromisin
  108. Mastiphen
  109. Mediamycetine
  110. Medichol
  111. Micloretin
  112. Micochlorine
  113. Micoclorina
  114. Microcetina
  115. Mychel
  116. Mychel-Vet
  117. Mycinol
  118. Normimycin V
  119. Novochlorocap
  120. Novomycetin
  121. Novophenicol
  122. Ocu-Chlor Ophthalmic Ointment
  123. Ocu-Chlor Ophthalmic Solution
  124. Oftalent
  125. Oleomycetin
  126. Opclor
  127. Opelor
  128. Ophtho-Chloram Ophthalmic Solution
  129. Ophthochlor
  130. Ophthochlor Ophthalmic Solution
  131. Ophthoclor
  132. Ophthocort
  133. Ophtochlor
  134. Optomycin
  135. Otachron
  136. Otophen
  137. Pantovernil
  138. Paraxin
  139. Pentamycetin
  140. Pentamycetin Ophthalmic Ointment
  141. Pentamycetin Ophthalmic Solution
  142. Quemicetina
  143. Rivomycin
  144. Romphenil
  145. Ronphenil
  146. Septicol
  147. Sificetina
  148. Sintomicetina
  149. Sintomicetine R
  150. Sno-Phenicol
  151. Sopamycetin Ophthalmic Ointment
  152. Sopamycetin Ophthalmic Solution
  153. Spectro-Chlor Ophthalmic Ointment
  154. Spectro-Chlor Ophthalmic Solution
  155. Stanomycetin
  156. Synthomycetin
  157. Synthomycetine
  158. Synthomycine
  159. Tega-Cetin
  160. Tevcocin
  161. Tevcosin
  162. Tifomycin
  163. Tifomycine
  164. Tiromycetin
  165. Treomicetina
  166. Tyfomycine
  167. Unimycetin
  168. Veticol
  169. Viceton
Brand Mixtures
  1. Actinac Pwr (Allantoin + Butoxyethyl Nicotinate + Chloramphenicol + Hydrocortisone Acetate + Sulfur)
  2. Actinac Pws (Allantoin + Butoxyethyl Nicotinate + Chloramphenicol + Hydrocortisone Acetate + Sulfur)
  3. Chlorasone (Chloramphenicol + Prednisolone Acetate)
  4. Elase Chloromycetin Ont (Chloramphenicol + Deoxyribonuclease Pancreatic + Fibrinolysin)
  5. Liquichlor (Chloramphenicol + Prednisolone + Squalane + Tetracaine)
  6. Ophthocort Ont (Chloramphenicol + Hydrocortisone Acetate + Polymyxin B)
  7. Sopamycetin/Hc Ointment (Chloramphenicol + Hydrocortisone Acetate)
  8. Sopamycetin/Hc Ont (Chloramphenicol + Hydrocortisone Acetate)
  9. Sopamycetin/Hc Susp (Chloramphenicol + Hydrocortisone Acetate)
  10. Zoomycetine Spray (Chloramphenicol + Isopropyl Alcohol + Methyl Violet)
Chemical IUPAC Name 2,2-dichloro-N-[1,3-dihydroxy-1-(4-nitrophenyl)propan-2-yl]acetamide
Chemical Formula C11H12Cl2N2O5
Chemical Structure Structure
CAS Registry Number 56-75-7
InChI Identifier InChI=1/C11H12Cl2N2O5/c12-10(13)11(18)14-8(5-16)9(17)6-1-3-7(4-2-6)15(19)20/h1-4,8-10,16-17H,5H2,(H,14,18)/f/h14H
InChI Key WIIZWVCIJKGZOK-YHMJCDSICC
KEGG Drug D00104 Link Image
KEGG Compound C00918 Link Image
PubChem Compound 298 Link Image
PubChem Substance 4172 Link Image
ChEBI ID 17698 Link Image
PharmGKB ID PA448927 Link Image
HET ID CLM Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00798398 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/chloramphenicol.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Chloramphenicol Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 323.1290
Monoisotopic Molecular Weight 322.0123
State Solid
Melting Point 150.5 oC
Experimental Water Solubility 2500 mg/L (at 25 °C) Source: PhysProp
Predicted Water Solubility 4.61e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.7 Source: PhysProp
Predicted LogP 1.15 Calculated using ALOGPS
Experimental LogS -2.11 [ADME Research, USCD]
Predicted LogS -2.85 Calculated using ALOGPS
Experimental Caco2 Permeability -4.69 [ADME Research, USCD]
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 3CLA Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES OC[C@H](NC(=O)C(Cl)Cl)[C@@H](O)C1=CC=C(C=C1)[N+]([O-])=O
Canonical SMILES OCC(NC(=O)C(Cl)Cl)C(O)C1=CC=C(C=C1)[N+]([O-])=O
Drug Category
  • Anti-Bacterial Agents
  • Protein Synthesis Inhibitors
ATC Codes
AHFS Codes
  • 08:12.08
  • 52:04.04
Indication Used in treatment of cholera, as it destroys the vibrios and decreases the diarrhea. It is effective against tetracycline-resistant vibrios. It is also used in eye drops or ointment to treat bacterial conjunctivitis.
Pharmacology Chloramphenicol is a broad-spectrum antibiotic that was derived from the bacterium Streptomyces venezuelae and is now produced synthetically. Chloramphenicol is effective against a wide variety of microorganisms, but due to serious side-effects (e.g., damage to the bone marrow, including aplastic anemia) in humans, it is usually reserved for the treatment of serious and life-threatening infections (e.g., typhoid fever). Chloramphenicol is bacteriostatic but may be bactericidal in high concentrations or when used against highly susceptible organisms. Chloramphenicol stops bacterial growth by binding to the bacterial ribosome (blocking peptidyl transferase) and inhibiting protein synthesis.
Mechanism of Action Chloramphenicol is lipid-soluble, allowing it to diffuse through the bacterial cell membrane. It then reversibly binds to the 50S subunit of bacterial ribosomes where transfer of amino acids to growing peptide chains is prevented (perhaps by suppression of peptidyl transferase activity), thus inhibiting peptide bond formation and subsequent protein synthesis.
Absorption Rapidly and completely absorbed from gastrointestinal tract following oral administration (bioavailability 80%). Well absorbed following intramuscular administration (bioavailability 70%). Intraocular and some systemic absorption also occurs after topical application to the eye.
Toxicity Oral, mouse: LD50 = 1500 mg/kg; Oral, rat: LD50 = 2500 mg/kg. Toxic reactions including fatalities have occurred in the premature and newborn; the signs and symptoms associated with these reactions have been referred to as the gray syndrome. Symptoms include (in order of appearance) abdominal distension with or without emesis, progressive pallid cyanosis, vasomotor collapse frequently accompanied by irregular respiration, and death within a few hours of onset of these symptoms.
Protein Binding Plasma protein binding is 50-60% in adults and 32% is premature neonates.
Biotransformation Hepatic, with 90% conjugated to inactive glucuronide.
Half Life Half-life in adults with normal hepatic and renal function is 1.5 - 3.5 hours. In patients with impaired renal function half-life is 3 - 4 hours. In patients with severely impaired hepatic function half-life is 4.6 - 11.6 hours. Half-life in children 1 month to 16 years old is 3 - 6.5 hours, while half-life in infants 1 to 2 days old is 24 hours or longer and is highly variable, especially in low birth-weight infants.
Dosage Forms
Form Route
Liquid Ophthalmic
Ointment Ophthalmic
Powder, for solution Intramuscular
Solution Ophthalmic
Solution / drops Ophthalmic
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Acenocoumarol Increases the anticoagulant effect
Acetohexamide The agent increases the effect of sulfonylurea
Anisindione Increases the anticoagulant effect
Chlorpropamide The agent increases the effect of sulfonylurea
Cyclosporine Increases the effect of cyclosporine
Dicumarol Increases the anticoagulant effect
Ethotoin Increases phenytoin, modifies chloramphenicol
Fosphenytoin Increases phenytoin, modifies chloramphenicol
Glibenclamide The agent increases the effect of sulfonylurea
Gliclazide The agent increases the effect of sulfonylurea
Glipizide The agent increases the effect of sulfonylurea
Glisoxepide The agent increases the effect of sulfonylurea
Glycodiazine The agent increases the effect of sulfonylurea
Mephenytoin Increases phenytoin, modifies chloramphenicol
Phenytoin Increases phenytoin, modifies chloramphenicol
Rifampin Rifampin decreases the effect of chloramphenicol
Tacrolimus Increases tacrolimus levels
Tolazamide The agent increases the effect of sulfonylurea
Tolbutamide The agent increases the effect of sulfonylurea
Warfarin Increases the anticoagulant effect
Food Interactions
  • Take on an empty stomach.
Pathways Not Available
General References
  1. Bhutta ZA, Niazi SK, Suria A: Chloramphenicol clearance in typhoid fever: implications for therapy. Indian J Pediatr. 1992 Mar-Apr;59(2):213-9. [PubMed Link Image]
  2. Nathan N, Borel T, Djibo A, Evans D, Djibo S, Corty JF, Guillerm M, Alberti KP, Pinoges L, Guerin PJ, Legros D: Ceftriaxone as effective as long-acting chloramphenicol in short-course treatment of meningococcal meningitis during epidemics: a randomised non-inferiority study. Lancet. 2005 Jul 23-29;366(9482):308-13. [PubMed Link Image]
  3. Pecoul B, Varaine F, Keita M, Soga G, Djibo A, Soula G, Abdou A, Etienne J, Rey M: Long-acting chloramphenicol versus intravenous ampicillin for treatment of bacterial meningitis. Lancet. 1991 Oct 5;338(8771):862-6. [PubMed Link Image]
  4. Wali SS, Macfarlane JT, Weir WR, Cleland PG, Ball PA, Hassan-King M, Whittle HC, Greenwood BM: Single injection treatment of meningococcal meningitis. 2. Long-acting chloramphenicol. Trans R Soc Trop Med Hyg. 1979;73(6):698-702. [PubMed Link Image]
  5. Puddicombe JB, Wali SS, Greenwood BM: A field trial of a single intramuscular injection of long-acting chloramphenicol in the treatment of meningococcal meningitis. Trans R Soc Trop Med Hyg. 1984;78(3):399-403. [PubMed Link Image]
  6. Wikipedia Link Image
  7. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. 50S ribosomal protein L10
  2. Complement decay-accelerating factor
  3. Chloramphenicol acetyltransferase
  4. Chloramphenicol 3-O phosphotransferase
  5. Chloramphenicol acetyltransferase 3
  6. Dr hemagglutinin structural subunit
Drug Target 1 [top]
Target 1 ID 818
Target 1 Name 50S ribosomal protein L10
Target 1 Synonyms Not Available
Target 1 Gene Name rplJ
Target 1 Protein Sequence >50S ribosomal protein L10 
ALNLQDKQAIVAEVSEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLLR
RAVEGTPFECLKDAFVGPTLIAYSMEHPGAAARLFKEFAKANAKFEVKAAAFEGELIPAS
QIDRLATLPTYEEAIARLMATMKEASAGKLVRTLAAVRDAKEAA
Target 1 Number of Residues 166
Target 1 Molecular Weight 17581
Target 1 Theoretical pI 9.51
Target 1 GO Classification
Function
structural molecule activity
structural constituent of ribosome
Process
metabolism
macromolecule metabolism
macromolecule biosynthesis
protein biosynthesis
physiological process
cellular physiological process
cell organization and biogenesis
organelle organization and biogenesis
ribosome biogenesis and assembly
Component
protein complex
ribonucleoprotein complex
ribosome
cell
intracellular
Target 1 General Function Translation, ribosomal structure and biogenesis
Target 1 Specific Function Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA
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 24054563 Link Image
Target 1 UniProtKB/Swiss-Prot ID P0A7J6 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name RL10_SHIFL Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >498 bp 
ATGGCTTTAAATCTTCAAGACAAACAAGCGATTGTTGCTGAAGTCAGCGAAGTAGCCAAA
GGCGCGCTGTCTGCAGTAGTTGCGGATTCCCGTGGCGTAACTGTAGATAAAATGACTGAA
CTGCGTAAAGCAGGTCGCGAAGCTGGCGTATACATGCGTGTTGTTCGTAACACCCTGCTG
CGCCGTGCTGTTGAAGGTACTCCGTTCGAGTGCCTGAAAGACGCGTTTGTTGGTCCGACC
CTGATTGCATACTCTATGGAACACCCGGGCGCTGCTGCTCGTCTGTTCAAAGAGTTCGCG
AAAGCGAATGCAAAATTTGAGGTCAAAGCCGCTGCCTTTGAAGGTGAGCTGATCCCGGCG
TCTCAGATCGACCGCCTGGCAACTCTGCCGACCTACGAAGAAGCAATTGCACGCCTGATG
GCAACCATGAAAGAAGCTTCGGCTGGCAAACTGGTTCGTACTCTGGCTGCTGTACGCGAT
GCGAAAGAAGCTGCTTAA
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. Jin Q, Yuan Z, Xu J, Wang Y, Shen Y, Lu W, Wang J, Liu H, Yang J, Yang F, Zhang X, Zhang J, Yang G, Wu H, Qu D, Dong J, Sun L, Xue Y, Zhao A, Gao Y, Zhu J, Kan B, Ding K, Chen S, Cheng H, Yao Z, He B, Chen R, Ma D, Qiang B, Wen Y, Hou Y, Yu J: Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157. Nucleic Acids Res. 2002 Oct 15;30(20):4432-41. [PubMed Link Image]
  2. Wei J, Goldberg MB, Burland V, Venkatesan MM, Deng W, Fournier G, Mayhew GF, Plunkett G 3rd, Rose DJ, Darling A, Mau B, Perna NT, Payne SM, Runyen-Janecky LJ, Zhou S, Schwartz DC, Blattner FR: Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun. 2003 May;71(5):2775-86. [PubMed Link Image]
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 1196
Target 2 Name Complement decay-accelerating factor
Target 2 Synonyms
  1. CD55 antigen
  2. Complement decay-accelerating factor precursor
Target 2 Gene Name CD55
Target 2 Protein Sequence >Complement decay-accelerating factor precursor 
MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTV
ITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFP
VGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGI
LFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGER
DHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPT
TVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLS
GHTCFTLTGLLGTLVTMGLLT
Target 2 Number of Residues 387
Target 2 Molecular Weight 41400
Target 2 Theoretical pI 7.64
Target 2 GO Classification Not Available
Target 2 General Function Not Available
Target 2 Specific Function Also acts as the receptor for echovirus 7 and related viruses (echoviruses 13, 21, 29 and 33)
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-34
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 181468 Link Image
Target 2 UniProtKB/Swiss-Prot ID P08174 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name DAF_HUMAN Link Image
Target 2 PDB ID 1OK9 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • GPI- anchor
  • Isoform 2:Cell membrane
  • lipid-anchor
Target 2 Gene Sequence >1146 bp 
ATGACCGTCGCGCGGCCGAGCGTGCCCGCGGCGCTGCCCCTCCTCGGGGAGCTGCCCCGG
CTGCTGCTGCTGGTGCTGTTGTGCCTGCCGGCCGTGTGGGGTGACTGTGGCCTTCCCCCA
GATGTACCTAATGCCCAGCCAGCTTTGGAAGGCCGTACAAGTTTTCCCGAGGATACTGTA
ATAACGTACAAATGTGAAGAAAGCTTTGTGAAAATTCCTGGCGAGAAGGACTCAGTGATC
TGCCTTAAGGGCAGTCAATGGTCAGATATTGAAGAGTTCTGCAATCGTAGCTGCGAGGTG
CCAACAAGGCTAAATTCTGCATCCCTCAAACAGCCTTATATCACTCAGAATTATTTTCCA
GTCGGTACTGTTGTGGAATATGAGTGCCGTCCAGGTTACAGAAGAGAACCTTCTCTATCA
CCAAAACTAACTTGCCTTCAGAATTTAAAATGGTCCACAGCAGTCGAATTTTGTAAAAAG
AAATCATGCCCTAATCCGGGAGAAATACGAAATGGTCAGATTGATGTACCAGGTGGCATA
TTATTTGGTGCAACCATCTCCTTCTCATGTAACACAGGGTACAAATTATTTGGCTCGACT
TCTAGTTTTTGTCTTATTTCAGGCAGCTCTGTCCAGTGGAGTGACCCGTTGCCAGAGTGC
AGAGAAATTTATTGTCCAGCACCACCACAAATTGACAATGGAATAATTCAAGGGGAACGT
GACCATTATGGATATAGACAGTCTGTAACGTATGCATGTAATAAAGGATTCACCATGATT
GGAGAGCACTCTATTTATTGTACTGTGAATAATGATGAAGGAGAGTGGAGTGGCCCACCA
CCTGAATGCAGAGGAAAATCTCTAACTTCCAAGGTCCCACCAACAGTTCAGAAACCTACC
ACAGTAAATGTTCCAACTACAGAAGTCTCACCAACTTCTCAGAAAACCACCACAAAAACC
ACCACACCAAATGCTCAAGCAACACGGAGTACACCTGTTTCCAGGACAACCAAGCATTTT
CATGAAACAACCCCAAATAAAGGAAGTGGAACCACTTCAGGTACTACCCGTCTTCTATCT
GGGCACACGTGTTTCACGTTGACAGGTTTGCTTGGGACGCTAGTAACCATGGGCTTGCTG
ACTTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID CD55 Link Image
Target 2 GenAtlas ID CD55 Link Image
Target 2 HGNC ID HGNC:2665 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1q32
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Uhrinova S, Lin F, Ball G, Bromek K, Uhrin D, Medof ME, Barlow PN: Solution structure of a functionally active fragment of decay-accelerating factor. Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4718-23. Epub 2003 Apr 2. [PubMed Link Image]
  2. Storry JR, Sausais L, Hue-Roye K, Mudiwa F, Ferrer Z, Blajchman MA, Lublin DM, Ma BW, Miquel JF, Nervi F, Pereira J, Reid ME: GUTI: a new antigen in the Cromer blood group system. Transfusion. 2003 Mar;43(3):340-4. [PubMed Link Image]
  3. Nakano Y, Sumida K, Kikuta N, Miura NH, Tobe T, Tomita M: Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen). Biochim Biophys Acta. 1992 Jun 12;1116(3):235-40. [PubMed Link Image]
  4. Ewulonu UK, Ravi L, Medof ME: Characterization of the decay-accelerating factor gene promoter region. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4675-9. [PubMed Link Image]
  5. Nakano Y, Sugita Y, Ishikawa Y, Choi NH, Tobe T, Tomita M: Isolation of two forms of decay-accelerating factor (DAF) from human urine. Biochim Biophys Acta. 1991 Jul 8;1074(2):326-30. [PubMed Link Image]
  6. Reid ME, Mallinson G, Sim RB, Poole J, Pausch V, Merry AH, Liew YW, Tanner MJ: Biochemical studies on red blood cells from a patient with the Inab phenotype (decay-accelerating factor deficiency). Blood. 1991 Dec 15;78(12):3291-7. [PubMed Link Image]
  7. Moran P, Raab H, Kohr WJ, Caras IW: Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site. J Biol Chem. 1991 Jan 15;266(2):1250-7. [PubMed Link Image]
  8. Sugita Y, Negoro T, Matsuda T, Sakamoto T, Tomita M: Improved method for the isolation and preliminary characterization of human DAF (decay-accelerating factor). J Biochem (Tokyo). 1986 Jul;100(1):143-50. [PubMed Link Image]
  9. Caras IW, Davitz MA, Rhee L, Weddell G, Martin DW Jr, Nussenzweig V: Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteins. Nature. 1987 Feb 5-11;325(6104):545-9. [PubMed Link Image]
  10. Medof ME, Lublin DM, Holers VM, Ayers DJ, Getty RR, Leykam JF, Atkinson JP, Tykocinski ML: Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc Natl Acad Sci U S A. 1987 Apr;84(7):2007-11. [PubMed Link Image]
  11. 7519480 Lublin DM, Mallinson G, Poole J, Reid ME, Thompson ES, Ferdman BR, Telen MJ, Anstee DJ, Tanner MJ: Molecular basis of reduced or absent expression of decay-accelerating factor in Cromer blood group phenotypes. Blood. 1994 Aug 15;84(4):1276-82.
  12. 7525274 Ward T, Pipkin PA, Clarkson NA, Stone DM, Minor PD, Almond JW: Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method. EMBO J. 1994 Nov 1;13(21):5070-4.
Target 2 Drug References
  1. Pettigrew D, Anderson KL, Billington J, Cota E, Simpson P, Urvil P, Rabuzin F, Roversi P, Nowicki B, du Merle L, Le Bouguenec C, Matthews S, Lea SM: High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol. J Biol Chem. 2004 Nov 5;279(45):46851-7. Epub 2004 Aug 24. [PubMed Link Image]
  2. Korotkova N, Chattopadhyay S, Tabata TA, Beskhlebnaya V, Vigdorovich V, Kaiser BK, Strong RK, Dykhuizen DE, Sokurenko EV, Moseley SL: Selection for functional diversity drives accumulation of point mutations in Dr adhesins of Escherichia coli. Mol Microbiol. 2007 Apr;64(1):180-94. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 2417
Target 3 Name Chloramphenicol acetyltransferase
Target 3 Synonyms
  1. EC 2.3.1.28
  2. XAT
  3. Xenobiotic acetyltransferase
Target 3 Gene Name cat
Target 3 Protein Sequence >Chloramphenicol acetyltransferase 
MGNYFESPFRGKLLSEQVSNPNIRVGRYSYYSGYYHGHSFDDCARYLMPDRDDVDKLVIG
SFCSIGSGAAFIMAGNQGHRAEWASTFPFHFMHEEPVFAGAVNGYQPAGDTLIGHDVWIG
TEAMFMPGVRVGHGAIIGSRALVTGDVEPYAIVGGNPARTIRKRFSDGDIQNLLEMAWWD
WPLADIEAAMPLLCTGDIPALYRHWKQRQATA
Target 3 Number of Residues 215
Target 3 Molecular Weight 23525
Target 3 Theoretical pI 6.07
Target 3 GO Classification Not Available
Target 3 General Function Involved in acyltransferase activity
Target 3 Specific Function This enzyme is an effector of chloramphenicol (Cm) resistance in bacteria. Acetylates Cm but not 1-acetoxy-Cm
Target 3 Pathways Not Available
Target 3 Reactions
  • acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
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 4104539 Link Image
Target 3 UniProtKB/Swiss-Prot ID P26841 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name CAT4_PSEAE Link Image
Target 3 PDB ID 2XAT Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >639 bp 
ATGGGCAACTATTTCGAGAGCCCCTTCAGGGGCAAGCTGCTCTCGGAACAGGTCAGCAAC
CCGAACATACGGGTGGGGCGCTACAGCTACTACTCCGGCTACTATCACGGGCATTCCTTC
GACGACTGCGCCCGCTACCTGATGCCGGACCGCGACGACGTGGACAAGCTGGTCATCGGC
AGTTTCTGCTCGATCGGCAGTGGCGCCGCCTTCATCATGGCCGGCAACCAGGGACACCGC
GCCGAATGGGCGTCGACCTTCCCCTTCCACTTCATGCACGAAGAGCCTGTCTTCGCCGGC
GCCGTGAACGGCTATCAGCCAGCCGGCGACACGCTGATCGGCCATGACGTCTGGATCGGT
ACCGAGGCGATGTTCATGCCCGGCGTACGGGTCGGCCACGGAGCCATCATCGGCAGCCGC
GCGCTGGTGACCGGCGATGTCGAGCCCTATGCCATCGTCGGCGGTAACCCGGCCCGGACC
ATTCGTAAGCGCTTTTCCGATGGCGATATCCAGAACCTGCTGGAAATGGCCTGGTGGGAC
TGGCCACTGGCCGATATCGAGGCAGCCATGCCACTGCTGTGTACTGGGGATATCCCCGCC
TTGTACCGGCACTGGAAACAGCGCCAGGCCACGGCCTGA
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 SNPJam Report Link Image
Target 3 General References
  1. White PA, Stokes HW, Bunny KL, Hall RM: Characterisation of a chloramphenicol acetyltransferase determinant found in the chromosome of Pseudomonas aeruginosa. FEMS Microbiol Lett. 1999 Jun 1;175(1):27-35. [PubMed Link Image]
  2. Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [PubMed Link Image]
  3. Hindahl MS, Frank DW, Hamood A, Iglewski BH: Characterization of a gene that regulates toxin A synthesis in Pseudomonas aeruginosa. Nucleic Acids Res. 1988 Jun 24;16(12):5699. [PubMed Link Image]
  4. Tian Y, Beaman TW, Roderick SL: Purification and crystallization of Pseudomonas aeruginosa chloramphenicol acetyltransferase. Proteins. 1997 Jun;28(2):298-300. [PubMed Link Image]
  5. Beaman TW, Sugantino M, Roderick SL: Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa. Biochemistry. 1998 May 12;37(19):6689-96. [PubMed Link Image]
Target 3 Drug References
  1. Navia MM, Capitano L, Ruiz J, Vargas M, Urassa H, Schellemberg D, Gascon J, Vila J: Typing and characterization of mechanisms of resistance of Shigella spp. isolated from feces of children under 5 years of age from Ifakara, Tanzania. J Clin Microbiol. 1999 Oct;37(10):3113-7. [PubMed Link Image]
  2. Potrykus J, Wegrzyn G: Chloramphenicol-sensitive Escherichia coli strain expressing the chloramphenicol acetyltransferase (cat) gene. Antimicrob Agents Chemother. 2001 Dec;45(12):3610-2. [PubMed Link Image]
  3. Potrykus J, Baranska S, Wegrzyn G: Inactivation of the acrA gene is partially responsible for chloramphenicol sensitivity of Escherichia coli CM2555 strain expressing the chloramphenicol acetyltransferase gene. Microb Drug Resist. 2002 Fall;8(3):179-85. [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]
Drug Target 4 [top]
Target 4 ID 2718
Target 4 Name Chloramphenicol 3-O phosphotransferase
Target 4 Synonyms
  1. CPT
  2. EC 2.7.1.-
Target 4 Gene Name Not Available
Target 4 Protein Sequence >Chloramphenicol 3-O phosphotransferase 
MTTRMIILNGGSSAGKSGIVRCLQSVLPEPWLAFGVDSLIEAMPLKMQSAEGGIEFDADG
GVSIGPEFRALEGAWAEGVVAMARAGARIIIDDVFLGGAAAQERWRSFVGDLDVLWVGVR
CDGAVAEGRETARGDRVAGMAAKQAYVVHEGVEYDVEVDTTHKESIECAWAIAAHVVP
Target 4 Number of Residues 180
Target 4 Molecular Weight 18817
Target 4 Theoretical pI 4.38
Target 4 GO Classification Not Available
Target 4 General Function Not Available
Target 4 Specific Function Inactivates chloramphenicol by catalyzing the transfer of the gamma-phosphate of ATP to the antibiotic's C-3' hydroxyl group
Target 4 Pathways Not Available
Target 4 Reactions Not Available
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 498888 Link Image
Target 4 UniProtKB/Swiss-Prot ID Q56148 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name CPT_STRVL Link Image
Target 4 PDB ID 1GRR Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >537 bp 
GTGACCACTCGGATGATCATCCTCAACGGCGGTTCCAGCGCGGGGAAGTCCGGCATCGTA
CGGTGCCTCCAGTCCGTCCTTCCCGAGCCCTGGCTGGCCTTCGGCGTCGACTCCCTCATC
GAGGCGATGCCCCTGAAGATGCAGAGCGCCGAAGGCGGCATCGAGTTCGACGCCGACGGC
GGGGTGAGCATCGGGCCCGAGTTCCGCGCCCTTGAGGGCGCCTGGGCCGAGGGCGTCGTC
GCGATGGCCCGCGCGGGCGCCCGGATCATCATCGACGACGTCTTCCTCGGCGGTGCCGCC
GCCCAGGAGCGCTGGCGGAGCTTCGTCGGGGACCTGGACGTGCTCTGGGTCGGCGTCCGG
TGCGACGGCGCCGTCGCCGAGGGCCGGGAGACCGCGCGCGGCGACCGCGTCGCGGGCATG
GCGGCGAAGCAGGCGTACGTCGTGCACGAGGGCGTGGAGTACGACGTGGAGGTCGACACC
ACGCACAAGGAGTCGATCGAGTGCGCCTGGGCGATCGCCGCCCACGTCGTCCCGTAG
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. Izard T, Ellis J: The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism. EMBO J. 2000 Jun 1;19(11):2690-700. [PubMed Link Image]
  2. Mosher RH, Camp DJ, Yang K, Brown MP, Shaw WV, Vining LC: Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer. J Biol Chem. 1995 Nov 10;270(45):27000-6. [PubMed Link Image]
Target 4 Drug References
  1. Ellis J, Campopiano DJ, Izard T: Cubic crystals of chloramphenicol phosphotransferase from Streptomyces venezuelae in complex with chloramphenicol. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1086-8. [PubMed Link Image]
  2. Izard T, Ellis J: The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism. EMBO J. 2000 Jun 1;19(11):2690-700. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Mosher RH, Camp DJ, Yang K, Brown MP, Shaw WV, Vining LC: Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer. J Biol Chem. 1995 Nov 10;270(45):27000-6. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 2808
Target 5 Name Chloramphenicol acetyltransferase 3
Target 5 Synonyms
  1. Chloramphenicol acetyltransferase III
  2. EC 2.3.1.28
  3. catIII
Target 5 Gene Name cat3
Target 5 Protein Sequence >Chloramphenicol acetyltransferase 3 
MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPVMIYLIAQ
AVNQFDELRMAIKDDELIVWDSVDPQFTVFHQETETFSALSCPYSSDIDQFMVNYLSVME
RYKSDTKLFPQGVTPENHLNISALPWVNFDSFNLNVANFTDYFAPIITMAKYQQEGDRLL
LPLSVQVHHAVCDGFHVARFINRLQELCNSKLK
Target 5 Number of Residues 216
Target 5 Molecular Weight 24994
Target 5 Theoretical pI 6.15
Target 5 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring groups other than amino-acyl groups
acyltransferase activity
O-acyltransferase activity
O-acetyltransferase activity
chloramphenicol O-acetyltransferase activity
Process
Not Available
Component
Not Available
Target 5 General Function Involved in chloramphenicol O-acetyltransferase activity
Target 5 Specific Function This enzyme is an effector of chloramphenicol resistance in bacteria
Target 5 Pathways Not Available
Target 5 Reactions
  • acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Essential
Target 5 GenBank ID Protein 47025 Link Image
Target 5 UniProtKB/Swiss-Prot ID P00484 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name CAT3_ECOLI Link Image
Target 5 PDB ID 3CLA Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location Not Available
Target 5 Gene Sequence >642 bp 
ATGAACTATACAAAATTTGATGTAAAAAATTGGGTTCGCCGTGAGCATTTTGAGTTTTAT
CGGCATCGTTTACCATGTGGTTTTAGCTTAACAAGCAAAATTGATATCACGACGTTAAAA
AAGTCATTGGATGATTCAGCGTATAAGTTTTATCCGGTAATGATCTATCTGATTGCTCAG
GCCGTGAATCAATTTGATGAGTTGAGAATGGCGATAAAAGATGATGAATTGATCGTATGG
GATTCAGTCGACCCACAATTCACCGTATTCCATCAAGAAACAGAGACATTTTCAGCACTG
AGTTGCCCATACTCATCCGATATTGATCAATTTATGGTGAATTATTTATCGGTAATGGAA
CGTTATAAAAGTGATACCAAGTTATTTCCTCAAGGGGTAACACCAGAAAATCATTTAAAT
ATTTCAGCATTACCTTGGGTTAATTTTGATAGCTTTAATTTAAATGTTGCTAATTTTACC
GATTATTTTGCACCCATTATAACAATGGCAAAATATCAGCAAGAAGGGGATAGACTGTTA
TTGCCGCTCTCAGTACAGGTTCATCATGCAGTTTGTGATGGCTTCCATGTTGCACGCTTT
ATTAATCGGCTACAAGAGTTGTGTAACAGTAAATTAAAATAA
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. Leslie AG: Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution. J Mol Biol. 1990 May 5;213(1):167-86. [PubMed Link Image]
  2. Murray IA, Hawkins AR, Keyte JW, Shaw WV: Nucleotide sequence analysis and overexpression of the gene encoding a type III chloramphenicol acetyltransferase. Biochem J. 1988 May 15;252(1):173-9. [PubMed Link Image]
  3. Leslie AG, Moody PC, Shaw WV: Structure of chloramphenicol acetyltransferase at 1.75-A resolution. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4133-7. [PubMed Link Image]
Target 5 Drug References
  1. Derrick JP, Lian LY, Roberts GC, Shaw WV: Analysis of the binding of 1,3-diacetylchloramphenicol to chloramphenicol acetyltransferase by isotope-edited 1H NMR and site-directed mutagenesis. Biochemistry. 1992 Sep 8;31(35):8191-5. [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. Murray IA, Lewendon A, Shaw WV: Stabilization of the imidazole ring of His-195 at the active site of chloramphenicol acetyltransferase. J Biol Chem. 1991 Jun 25;266(18):11695-8. [PubMed Link Image]
  5. Murray IA, Cann PA, Day PJ, Derrick JP, Sutcliffe MJ, Shaw WV, Leslie AG: Steroid recognition by chloramphenicol acetyltransferase: engineering and structural analysis of a high affinity fusidic acid binding site. J Mol Biol. 1995 Dec 15;254(5):993-1005. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 2810
Target 6 Name Dr hemagglutinin structural subunit
Target 6 Synonyms
  1. Dr hemagglutinin structural subunit precursor
Target 6 Gene Name draA
Target 6 Protein Sequence >Dr hemagglutinin structural subunit precursor 
MKKLAIMAAASMVFAVSSAHAGFTPSGTTGTTKLTVTEECQVRVGDLTVAKTRGQLTDAA
PIGPVTVQALGCDARQVALKADTDNFEQGKFFLISDNNRDKLYVNIRPTDNSAWTTDNGV
FYKNDVGSWGGIIGIYVDGQQTNTPPGNYTLTLTGGYWAK
Target 6 Number of Residues 162
Target 6 Molecular Weight 17058
Target 6 Theoretical pI 7.25
Target 6 GO Classification
Function
binding
protein binding
Process
Not Available
Component
Not Available
Target 6 General Function Involved in protein binding
Target 6 Specific Function Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA))
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • 1-21
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Essential
Target 6 GenBank ID Protein 145801 Link Image
Target 6 UniProtKB/Swiss-Prot ID P24093 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name FMDR_ECOLI Link Image
Target 6 PDB ID 1UT1 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cell projection
  • fimbrium
Target 6 Gene Sequence >483 bp 
ATGAAAAAATTAGCGATCATGGCCGCGGCCAGCATGGTGTTCGCCGTGAGCTCCGCGCAT
GCTGGGTTCACCCCGAGTGGCACCACCGGCACCACCAAACTCACAGTTACCGAAGAGTGC
CAGGTACGGGTTGGTGACCTGACCGTGGCTAAGACTCGTGGCCAACTGACGGACGCAGCA
CCAATAGGGCCGGTCACCGTGCAAGCGCTGGGATGCGACGCCCGCCAGGTCGCGTTGAAG
GCAGACACCGATAACTTCGAACAGGGCAAGTTCTTCCTGATCAGCGACAACAATAGGGAT
AAGCTCTATGTCAATATACGGCCTACGGATAACTCCGCCTGGACGACCGACAATGGTGTC
TTCTACAAAAACGATGTCGGGAGCTGGGGTGGAATTATCGGGATCTACGTAGATGGGCAA
CAAACGAACACACCGCCCGGCAACTACACACTGACCCTGACCGGGGGTTACTGGGCAAAA
TGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID Not Available
Target 6 GenAtlas ID Not Available
Target 6 HGNC ID Not Available
Target 6 Chromosome Location Not Available
Target 6 Locus Not Available
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Swanson TN, Bilge SS, Nowicki B, Moseley SL: Molecular structure of the Dr adhesin: nucleotide sequence and mapping of receptor-binding domain by use of fusion constructs. Infect Immun. 1991 Jan;59(1):261-8. [PubMed Link Image]
  2. Kist ML, Salit IE, Hofmann T: Purification and characterization of the Dr hemagglutinins expressed by two uropathogenic Escherichia coli strains. Infect Immun. 1990 Mar;58(3):695-702. [PubMed Link Image]
Target 6 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.