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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:50
Primary Accession Number DB00207
Secondary Accession Number
  • APRD00397
Name Azithromycin
Drug Type
  • Approved
  • Small Molecule
Description A semi-synthetic macrolide antibiotic structurally related to erythromycin. It has been used in the treatment of Mycobacterium avium intracellulare infections, toxoplasmosis, and cryptosporidiosis. [PubChem]
Synonyms
  1. Aritromicina [Spanish]
  2. Azithramycine
  3. Azithromycin Dihydrate
  4. Azithromycine [French]
  5. Azithromycinum [Latin]
Brand Names
  1. Azenil
  2. Azibiot
  3. Azifine
  4. Azitromax
  5. Aziwok
  6. Aztrin
  7. Hemomycin
  8. Misultina
  9. Mixoterin
  10. Setron
  11. Sumamed
  12. Tobil
  13. Tromix
  14. Vinzam
  15. Zeto
  16. Zifin
  17. Zithrax
  18. Zithromax
  19. Zitrim
  20. Zitrocin
  21. Zitromax
  22. Zitrotek
  23. Zmax
Brand Mixtures Not Available
Chemical IUPAC Name (2R,3S,4R,5R,8R,10R,11R,13S,14R)-11-[(2S,3R,4S,6R)-4-dimethylamino-3-hydroxy-6-methyloxan-2-yl]oxy-2-ethyl-3,4,10-trihydroxy-13-[(2R,4R,5S,6S)-5-hydroxy-4-methoxy-4,6-dimethyloxan-2-yl]oxy-3,5,6,8,10,12,14-heptamethyl-1-oxa-6-azacyclopentadecan-15-one
Chemical Formula C38H72N2O12
Chemical Structure Structure
CAS Registry Number 83905-01-5
InChI Identifier InChI=1/C38H72N2O12/c1-15-27-38(10,46)31(42)24(6)40(13)19-20(2)17-36(8,45)33(52-35-29(41)26(39(11)12)16-21(3)48-35)22(4)30(23(5)34(44)50-27)51-28-18-37(9,47-14)32(43)25(7)49-28/h20-33,35,41-43,45-46H,15-19H2,1-14H3/t20-,21-,22?,23-,24-,25+,26+,27-,28+,29-,30+,31-,32+,33-,35+,36-,37-,38-/m1/s1
InChI Key MQTOSJVFKKJCRP-OHJWJPDZBP
KEGG Drug Not Available
KEGG Compound C06838 Link Image
PubChem Compound 55185 Link Image
PubChem Substance 9056 Link Image
ChEBI ID Not Available
PharmGKB ID PA448519 Link Image
HET ID ZIT Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02255340 Link Image
RxList Link http://www.rxlist.com/cgi/generic/zithromax.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Azithromycin Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference G.Kobrehel, S.Djokic, U.S. pat. 4,517,359 (1982, 1985 to Sour Pliva)
Average Molecular Weight 748.9845
Monoisotopic Molecular Weight 748.5085
State Solid
Melting Point 113-115 oC
Experimental Water Solubility slight Source: PhysProp
Predicted Water Solubility 5.14e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 4.02 [MCFARLAND,JW ET AL. (1997)] Source: PhysProp
Predicted LogP 3.03 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.16 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 8.74
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 CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@H]2C[C@@](C)(OC)[C@@H](O)[C@H](C)O2)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@@H]([C@H]2O)N(C)C)[C@](C)(O)C[C@@H](C)CN(C)[C@H](C)[C@@H](O)[C@]1(C)O
Canonical SMILES CCC1OC(=O)C(C)C(OC2CC(C)(OC)C(O)C(C)O2)C(C)C(OC2OC(C)CC(C2O)N(C)C)C(C)(O)CC(C)CN(C)C(C)C(O)C1(C)O
Drug Category
  • Anti-Bacterial Agents
  • Macrolides
  • Other Macrolides
ATC Codes
AHFS Codes
  • 08:12.12.92
Indication For the treatment of patients with mild to moderate infections caused by susceptible strains of the designated microorganisms in the specific conditions: H. influenzae, M. catarrhalis, S. pneumoniae, C. pneumoniae, M. pneumoniae, S. pyogenes, S. aureus, S. agal
Pharmacology Azithromycin, a semisynthetic antibiotic belonging to the macrolide subgroup of azalides, is used to treat STDs due to chlamydia and gonorrhea, community-acquired pneumonia, pelvic inflammatory disease, pediatric otitis media and pharyngitis, and Mycobacterium avium complex (MAC) in patients with advanced HIV disease. Similar in structure to erythromycin. azithromycin reaches higher intracellular concentrations than erythromycin, increasing its efficacy and duration of action.
Mechanism of Action Azithromycin binds to the 50S subunit of the 70S bacterial ribosomes, and therefore inhibits RNA-dependent protein synthesis in bacterial cells.
Absorption Bioavailability is 37% following oral administration.
Toxicity Potentially serious side effects of angioedema and cholestatic jaundice were reported
Protein Binding Serum protein binding is variable in the concentration range approximating human exposure, decreasing from 51% at 0.02 µg/mL to 7% at 2 µg/mL.
Biotransformation Hepatic. In vitro and in vivo studies to assess the metabolism of azithromycin have not been performed.
Half Life 68 hours
Dosage Forms
Form Route
Powder, for solution Intravenous
Powder, for solution Oral
Powder, for suspension Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol Increases the anticoagulant effect
Anisindione Increases the anticoagulant effect
Cyclosporine The macrolide increases the effect of cyclosporine
Dicumarol Increases the anticoagulant effect
Disopyramide The macrolide increases the effect of disopyramide
Lovastatin Azithromycin can possibly increase the statin toxicity
Warfarin Increases the anticoagulant effect
Food Interactions
  • Do not take Aluminum or magnesium antacids or supplements while on this medication.
  • Take on empty stomach: 1 hour before or 2 hours after meals.
Pathways
Name SMPDB Link KEGG Link
Azithromycin Pathway SMP00247 Link Image
General References
  1. Noedl H, Krudsood S, Chalermratana K, Silachamroon U, Leowattana W, Tangpukdee N, Looareesuwan S, Miller RS, Fukuda M, Jongsakul K, Sriwichai S, Rowan J, Bhattacharyya H, Ohrt C, Knirsch C: Azithromycin combination therapy with artesunate or quinine for the treatment of uncomplicated Plasmodium falciparum malaria in adults: a randomized, phase 2 clinical trial in Thailand. Clin Infect Dis. 2006 Nov 15;43(10):1264-71. Epub 2006 Oct 12. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. 23S rRNA
  2. 50S ribosomal protein L22
  3. 50S ribosomal protein L4
Drug Target 1 [top]
Target 1 ID 884
Target 1 Name 23S rRNA
Target 1 Synonyms
  1. 23S ribosomal ribonucleic acid
Target 1 Gene Name Not Available
Target 1 Protein Sequence Not Available
Target 1 Number of Residues 0
Target 1 Molecular Weight Not Available
Target 1 Theoretical pI Not Available
Target 1 GO Classification
Function
transferase activity
translation
RNA binding
Process
rRNA processing
RNA processing and modification
Component
cell
Target 1 General Function Translation, ribosomal structure and biogenesis
Target 1 Specific Function In prokaryotes, the 23S rRNA is part of the large subunit (the 50S) that joins with the 30S small subunit to create the functional 70S ribosome. The ribosome is comprised of 3 RNAs: the 23S, the 16S and the 5S ribosomal RNAs. The 23S and the 5S associate with their respective proteins to make up the large subunit of the ribosome, while the 16S RNA associates with its proteins to make up the small subunit.
Target 1 Pathways
Name SMPDB Link KEGG Link
Ribosome map03010 Link Image
Target 1 Reactions
  • tRNA-aminoacid + ATP + polypeptide(n) = polypeptide(n+1) + ADP
Target 1 Pfam Domain Function Not Available
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein Not Available
Target 1 UniProtKB/Swiss-Prot ID Not Available
Target 1 UniProtKB/Swiss-Prot Entry Name Not Available
Target 1 PDB ID 1EMI Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >23S rRNA sequence 
GATTAAGTTATTAAGGGCGCACGGTGGATGCCTTGGCACTAGAAGCCGATGAAGGACGTT
ACTAACGACGATATGCTTTGGGGAGCTGTAAGTAAGCTTTGATCCAGAGATTTCCGAATG
GGGAAACCCAGCATGAGTTATGTCATGTTATCGATATGTGAATACATAGCATATCAGAAG
GCACACCCGGAGAACTGAAACATCTTAGTACCCGGAGGAAGAGAAAGAAAATTCGATTCC
CTTAGTAGCGGCGAGCGAAATGGGAAGAGCCCAAACCAACAAGCTTGCTTGTTGGGGTTG
TAGGACACTCTATACGGAGTTACAAAGGACGACATTAGACGAATCATCTGGAAAGATGAA
TCAAAGAAGGTAATAATCCTGTAGTCGAAAATGTTGTCTCTCTTGAGTGGATCCTGAGTA
CGACGGAGCACGTGAAATTCCGTCGGAATCTGGGAGGACCATCTCCTAAGGCTAAATACT
CTCTAGTGACCGATAGTGAACCAGTACCGTGAGGGAAAGGTGAAAAGCACCCCGGAAGGG
GAGTGAAATAGAACCTGAAACCGTGTGCTTACAAGTAGTCAGAGCCCGTTAATGGGTGAT
GGCGTGCCTTTTGTAGAATGAACCGGCGAGTTACGATTTGATGCAAGGTTAAGCAGTAAA
TGTGGAGCCGTAGCGAAAGCGAGTCTGAATAGGGCGTTTAGTATTTGGTCGTAGACCCGA
AACCAGGTGATCTACCCTTGGTCAGGTTGAAGTTCAGGTAACACTGAATGGAGGACCGAA
CCGACTTACGTTGAAAAGTGAGCGGATGAACTGAGGGTAGCGGAGAAATTCCAATCGAAC
CTGGAGATAGCTGGTTCTCTCCGAAATAGCTTTAGGGCTAGCCTCAAGTGATGATTATTG
GAGGTAGAGCACTGTTTGGACGAGGGGCCCCTCTCGGGTTACCGAATTCAGACAAACTCC
GAATGCCAATTAATTTAACTTGGGAGTCAGAACATGGGTGATAAGGTCCGTGTTCGAAAG
GGAAACAGCCCAGACCACCAGCTAAGGTCCCAAAATATATGTTAAGTGGAAAAGGATGTG
GCGTTGCCCAGACAACTAGGATGTTGGCTTAGAAGCAGCCATCATTTAAAGAGTGCGTAA
TAGCTCACTAGTCGAGTGACACTGCGCCGAAAATGTACCGGGGCTAAACATATTACCGAA
GCTGTGGATTGTCCTTTGGACAATGGTAGGAGAGCGTTCTAAGGGCGTTGAAGCATGATC
GTAAGGACATGTGGAGCGCTTAGAAGTGAGAATGCCGGTGTGAGTAGCGAAAGACGGGTG
AGAATCCCGTCCACCGATTGACTAAGGTTTCCAGAGGAAGGCTCGTCCGCTCTGGGTTAG
TCGGGTCCTAAGCTGAGGCCGACAGGCGTAGGCGATGGATAACAGGTTGATATTCCTGTA
CCACCTATAATCGTTTTAATCGATGGGGGGACGCAGTAGGATAGGCGAAGCGTGCGATTG
GATTGCACGTCTAAGCAGTAAGGCTGAGTATTAGGCAAATCCGGTACTCGTTAAGGCTGA
GCTGTGATGGGGAGAAGACATTGTGTCTTCGAGTCGTTGATTTCACACTGCCGAGAAAAG
CCTCTAGATAGAAAATAGGTGCCCGTACCGCAAACCGACACAGGTAGTCAAGATGAGAAT
TCTAAGGTGAGCGAGCGAACTCTCGTTAAGGAACTCGGCAAAATGACCCCGTAACTTCGG
GAGAAGGGGTGCTCTTTAGGGTTAACGCCCAGAAGAGCCGCAGTGAATAGGCCCAAGCGA
CTGTTTATCAAAAACACAGGTCTCTGCTAAACCGTAAGGTGATGTATAGGGGCTGACGCC
TGCCCGGTGCTGGAAGGTTAAGAGGAGTGGTTAGCTTCTGCGAAGCTACGAATCGAAGCC
CCAGTAAACGGCGGCCGTAACTATAACGGTCCTAAGGTAGCGAAATTCCTTGTCGGGTAA
GTTCCGACCCGCACGAAAGGCGTAACGATTTGGGCACTGTCTCAACGAGAGACTCGGTGA
AATCATAGTACCTGTGAAGATGCAGGTTACCCGCGACAGGACGGAAAGACCCCGTGGAGC
TTTACTGTAGCCTGATATTGAAATTCGGCACAGCTTGTACAGGATAGGTAGGAGCCTTTG
AAACGTGAGCGCTAGCTTACGTGGAGGCGCTGGTGGGATACTACCCTAGCTGTGTTGGCT
TTCTAACCCGCACCACTTATCGTGGTGGGAGACAGTGTCAGGCGGGCAGTTTGACTGGGG
CGGTCGCCTCCTAAAAGGTAACGGAGGCGCTCAAAGGTTCCCTCAGAATGGTTGGAAATC
ATTCATAGAGTGTAAAGGCATAAGGGAGCTTGACTGCGAGACCTACAAGTCGAGCAGGGT
CGAAAGACGGACTTAGTGATCCGGTGGTTCCGCATGGAAGGGCCATCGCTCAACGGATAA
AAGCTACCCCGGGGATAACAGGCTTATCTCCCCCAAGAGTTCACATCGACGGGGAGGTTT
GGCACCTCGATGTCGGCTCATCGCATCCTGGGGCTGTAGTCGGTCCCAAGGGTTGGGCTG
TTCGCCCATTAAAGCGGTACGCGAGCTGGGTTCAGAACGTCGTGAGACAGTTCGGTCCCT
ATCCGTCGTGGGCGTAGGAAATTTGAGAGGAGCTGTCCTTAGTACGAGAGGACCGGGATG
GACATACCTCTGGTGTACCAGTTGTCGTGCCAACGGCATAGCTGGGTAGCTATGTGTGGA
CGGGATAAGTGCTGAAAGCATCTAAGCATGAAGCCCCCCTCAAGATGAGATTTCCCAACT
TCGGTTATAAGATCCCTCAAAGATGATGAGGTTAATAGGTTCGAGGTGGAAGCATGGTGA
CATGTGGAGCTGACGAATACTAATCGATCGAAGACTTAATCAA
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 Not Available
Target 1 General References
  1. Barrett JF: Linezolid Pharmacia Corp. Curr Opin Investig Drugs. 2000 Oct;1(2):181-7. [PubMed Link Image]
Target 1 Drug References
  1. Ng LK, Martin I, Liu G, Bryden L: Mutation in 23S rRNA associated with macrolide resistance in Neisseria gonorrhoeae. Antimicrob Agents Chemother. 2002 Sep;46(9):3020-5. [PubMed Link Image]
  2. Jalava J, Vaara M, Huovinen P: Mutation at the position 2058 of the 23S rRNA as a cause of macrolide resistance in Streptococcus pyogenes. Ann Clin Microbiol Antimicrob. 2004 May 6;3:5. [PubMed Link Image]
  3. Pereyre S, Renaudin H, Charron A, Bebear C, Bebear CM: Emergence of a 23S rRNA mutation in Mycoplasma hominis associated with a loss of the intrinsic resistance to erythromycin and azithromycin. J Antimicrob Chemother. 2006 Apr;57(4):753-6. Epub 2006 Feb 7. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 4237
Target 2 Name 50S ribosomal protein L22
Target 2 Synonyms Not Available
Target 2 Gene Name rplV
Target 2 Protein Sequence >50S ribosomal protein L22 
METIAKHRHARSSAQKVRLVADLIRGKKVSQALDILTYTNKKAAVLVKKVLESAIANAEH
NDGADIDDLKVTKIFVDEGPSMKRIMPRAKGRADRILKRTSHITVVVSDR
Target 2 Number of Residues 111
Target 2 Molecular Weight 12226
Target 2 Theoretical pI 10.98
Target 2 GO Classification
Function
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
large ribosomal subunit
Target 2 General Function Involved in structural constituent of ribosome
Target 2 Specific Function The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome (By similarity)
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 Not Available
Target 2 UniProtKB/Swiss-Prot ID P61177 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name RL22_ECO57 Link Image
Target 2 PDB ID 1P86 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >333 bp 
TCAGCGATCGGACACAACCACAGTGATGTGGCTGGTGCGCTTCAGGATGCGATCTGCACG
ACCTTTTGCACGCGGCATAATGCGCTTCATGCTCGGGCCTTCGTCTACGAAAATTTTCGT
AACTTTCAGATCGTCAATGTCAGCGCCATCGTTGTGTTCAGCGTTAGCAATGGCAGATTC
CAGAACTTTCTTGACCAGTACAGCCGCTTTCTTGTTGGTGTAGGTCAAAATATCCAGAGC
CTGCGACACTTTCTTACCGCGAATCAGGTCAGCAACAAGGCGAACCTTCTGAGCAGAAGA
ACGAGCATGGCGATGTTTAGCGATAGTTTCCAT
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. Perna NT, Plunkett G 3rd, Burland V, Mau B, Glasner JD, Rose DJ, Mayhew GF, Evans PS, Gregor J, Kirkpatrick HA, Posfai G, Hackett J, Klink S, Boutin A, Shao Y, Miller L, Grotbeck EJ, Davis NW, Lim A, Dimalanta ET, Potamousis KD, Apodaca J, Anantharaman TS, Lin J, Yen G, Schwartz DC, Welch RA, Blattner FR: Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature. 2001 Jan 25;409(6819):529-33. [PubMed Link Image]
  2. Hayashi T, Makino K, Ohnishi M, Kurokawa K, Ishii K, Yokoyama K, Han CG, Ohtsubo E, Nakayama K, Murata T, Tanaka M, Tobe T, Iida T, Takami H, Honda T, Sasakawa C, Ogasawara N, Yasunaga T, Kuhara S, Shiba T, Hattori M, Shinagawa H: Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12. DNA Res. 2001 Feb 28;8(1):11-22. [PubMed Link Image]
Target 2 Drug References
  1. Schlunzen F, Harms JM, Franceschi F, Hansen HA, Bartels H, Zarivach R, Yonath A: Structural basis for the antibiotic activity of ketolides and azalides. Structure. 2003 Mar;11(3):329-38. [PubMed Link Image]
  2. Tu D, Blaha G, Moore PB, Steitz TA: Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell. 2005 Apr 22;121(2):257-70. [PubMed Link Image]
  3. Halling SM, Jensen AE: Intrinsic and selected resistance to antibiotics binding the ribosome: analyses of Brucella 23S rrn, L4, L22, EF-Tu1, EF-Tu2, efflux and phylogenetic implications. BMC Microbiol. 2006 Oct 2;6:84. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 4238
Target 3 Name 50S ribosomal protein L4
Target 3 Synonyms Not Available
Target 3 Gene Name rplD
Target 3 Protein Sequence >50S ribosomal protein L4 
MELVLKDAQSALTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEVTGSGKKPW
RQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRGALKSILSELVRQDRLIV
VEKFSVEAPKTKLLAQKLKDMALEDVLIITGELDENLFLAARNLHKVDVRDATGIDPVSL
IAFDKVVMTADAVKQVEEMLA
Target 3 Number of Residues 204
Target 3 Molecular Weight 22087
Target 3 Theoretical pI 10.45
Target 3 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 3 General Function Involved in structural constituent of ribosome
Target 3 Specific Function Forms part of the polypeptide exit tunnel (By similarity)
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
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 P60725 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name RL4_ECO57 Link Image
Target 3 PDB ID 1P86 Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >606 bp 
TCATGCCAGCATCTCCTCAACTTGCTTAACAGCATCAGCAGTCATTACGACTTTGTCGAA
GGCGATCAGGCTAACCGGGTCGATACCAGTTGCATCGCGTACGTCAACCTTGTGCAGGTT
GCGCGCAGCCAGGAACAGGTTTTCGTCCAGCTCACCGGTGATGATCAGCACATCTTCCAG
AGCCATGTCTTTCAGTTTCTGTGCCAGCAGCTTAGTTTTCGGCGCTTCTACAGAGAACTT
CTCGACAACGATCAGACGATCCTGACGTACCAGTTCGGACAGGATGCTTTTCAGCGCGCC
GCGGTACATCTTCTTGTTAACTTTTTGACTGTGGTCCTGCGGACGAGCAGCAAAGGTCAC
GCCACCAGAACGCCAGATCGGGCTCTTGATAGAACCAGAACGCGCACGGCCGGTGCCTTT
CTGGCGCCACGGTTTTTTACCGGAACCAGTTACTTCAGCACGAGTCTTCTGAGCACGAGT
ACCCTGACGAGCACCAGCTGCATAAGCAACAACAACCTGGTGAACCAGCGCTTCGTTGAA
ATCACGACCGAAGGTAGTTTCGGAAACAGTCAGCGCGCTCTGCGCGTCTTTCAATACTAA
TTCCAT
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. Perna NT, Plunkett G 3rd, Burland V, Mau B, Glasner JD, Rose DJ, Mayhew GF, Evans PS, Gregor J, Kirkpatrick HA, Posfai G, Hackett J, Klink S, Boutin A, Shao Y, Miller L, Grotbeck EJ, Davis NW, Lim A, Dimalanta ET, Potamousis KD, Apodaca J, Anantharaman TS, Lin J, Yen G, Schwartz DC, Welch RA, Blattner FR: Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature. 2001 Jan 25;409(6819):529-33. [PubMed Link Image]
  2. Hayashi T, Makino K, Ohnishi M, Kurokawa K, Ishii K, Yokoyama K, Han CG, Ohtsubo E, Nakayama K, Murata T, Tanaka M, Tobe T, Iida T, Takami H, Honda T, Sasakawa C, Ogasawara N, Yasunaga T, Kuhara S, Shiba T, Hattori M, Shinagawa H: Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12. DNA Res. 2001 Feb 28;8(1):11-22. [PubMed Link Image]
Target 3 Drug References
  1. Schlunzen F, Harms JM, Franceschi F, Hansen HA, Bartels H, Zarivach R, Yonath A: Structural basis for the antibiotic activity of ketolides and azalides. Structure. 2003 Mar;11(3):329-38. [PubMed Link Image]
  2. Tu D, Blaha G, Moore PB, Steitz TA: Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell. 2005 Apr 22;121(2):257-70. [PubMed Link Image]
  3. Halling SM, Jensen AE: Intrinsic and selected resistance to antibiotics binding the ribosome: analyses of Brucella 23S rrn, L4, L22, EF-Tu1, EF-Tu2, efflux and phylogenetic implications. BMC Microbiol. 2006 Oct 2;6:84. [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.