| 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 |
|
| Name |
Azithromycin |
| Drug Type |
|
| 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 |
- Aritromicina [Spanish]
- Azithramycine
- Azithromycin Dihydrate
- Azithromycine [French]
- Azithromycinum [Latin]
|
| Brand Names |
- Azenil
- Azibiot
- Azifine
- Azitromax
- Aziwok
- Aztrin
- Hemomycin
- Misultina
- Mixoterin
- Setron
- Sumamed
- Tobil
- Tromix
- Vinzam
- Zeto
- Zifin
- Zithrax
- Zithromax
- Zitrim
- Zitrocin
- Zitromax
- Zitrotek
- 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 |
 |
| 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  |
| PubChem Compound |
55185  |
| PubChem Substance |
9056  |
| ChEBI ID |
Not Available |
| PharmGKB ID |
PA448519  |
| HET ID |
ZIT  |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
02255340  |
| RxList Link |
http://www.rxlist.com/cgi/generic/zithromax.htm  |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Azithromycin  |
| 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 | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 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 |
|
| 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  |
| Contraindications |
Show  |
| Interactions |
Show  |
| 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  |
|
|
| General References |
- 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
]
- Drugs.com

- Wikipedia

- RxList

|
| Organisms Affected |
- Enteric bacteria and other eubacteria
|
| Targets |
- 23S rRNA
- 50S ribosomal protein L22
- 50S ribosomal protein L4
|
|
Drug Target 1
[top]
|
| Target 1 ID |
884 |
| Target 1 Name |
23S rRNA |
| Target 1 Synonyms |
- 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  |
|
| Target 1 Reactions |
- tRNA-aminoacid + ATP + polypeptide(n) = polypeptide(n+1) + ADP
|
| Target 1 Pfam Domain Function |
Not Available |
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
|
| 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  |
| Target 1 PDB File |
Show |
| Target 1 3D Structure |
|
| Target 1 Cellular Location |
|
| 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 |
- Barrett JF: Linezolid Pharmacia Corp. Curr Opin Investig Drugs. 2000 Oct;1(2):181-7. [PubMed
]
|
| Target 1 Drug References |
- 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
]
- 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
]
- 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
]
|
|
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 |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Essential |
| Target 2 GenBank ID Protein |
Not Available |
| Target 2 UniProtKB/Swiss-Prot ID |
P61177  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
RL22_ECO57  |
| Target 2 PDB ID |
1P86  |
| 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  |
| Target 2 General References |
- 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
]
- 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
]
|
| Target 2 Drug References |
- 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
]
- 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
]
- 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
]
|
|
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 |
|
| Target 3 Transmembrane Regions |
|
| Target 3 Essentiality |
Essential |
| Target 3 GenBank ID Protein |
Not Available |
| Target 3 UniProtKB/Swiss-Prot ID |
P60725  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
RL4_ECO57  |
| Target 3 PDB ID |
1P86  |
| 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  |
| Target 3 General References |
- 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
]
- 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
]
|
| Target 3 Drug References |
- 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
]
- 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
]
- 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
]
|