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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 DB00199
Secondary Accession Number
  • APRD00953
Name Erythromycin
Drug Type
  • Approved
  • Small Molecule
Description Erythromycin is a bacteriostatic antibiotic macrolide produced by Streptomyces erythreus. Erythromycin A is considered its major active component. In sensitive organisms, it inhibits protein synthesis by binding to 50S ribosomal subunits. This binding process inhibits peptidyl transferase activity and interferes with translocation of amino acids during translation and assembly of proteins. [PubChem]
Synonyms
  1. EM
  2. Erythrocin
  3. Erythrocin Stearate
  4. Erythromycin Stearate
  5. Erythromycin estolate
  6. Erythromycin ethylsuccinate
  7. Erythromycin glucoheptonate
  8. Erythromycin lactobionate
  9. Erythromycin oxime
Brand Names
  1. Abboticin
  2. Abomacetin
  3. Ak-mycin
  4. Akne-Mycin
  5. Aknin
  6. Benzamycin
  7. Benzamycin Pak
  8. Bristamycin
  9. Dotycin
  10. Dumotrycin
  11. E-Base
  12. E-Glades
  13. E-Mycin
  14. E-Solve 2
  15. EMU
  16. ETS
  17. Emgel
  18. Eritrocina
  19. Ermycin
  20. Ery-Sol
  21. Ery-Tab
  22. Eryc
  23. Eryc 125
  24. Eryc Sprinkles
  25. Erycen
  26. Erycette
  27. Erycin
  28. Erycinum
  29. Eryderm
  30. Erygel
  31. Erymax
  32. Erypar
  33. Erythra-Derm
  34. Erythro
  35. Erythro-Statin
  36. Erythrogran
  37. Erythroguent
  38. Erythromast 36
  39. Erythromid
  40. Erythromycin A
  41. Erythromycin B
  42. Ethril 250
  43. Ilocaps
  44. Ilosone
  45. Ilotycin
  46. Ilotycin Gluceptate
  47. IndermRetcin
  48. Kesso-Mycin
  49. Mephamycin
  50. Pantomicina
  51. Pce
  52. Pfizer-e
  53. Propiocine
  54. R-P Mycin
  55. Robimycin
  56. Sansac
  57. Serp-AFD
  58. Stiemycin
  59. Taimoxin-F
  60. Theramycin Z
  61. Torlamicina
  62. Wemid
  63. Wyamycin S
Brand Mixtures
  1. Sans-Acne Solution (Alcohol Anhydrous + Erythromycin)
  2. Staticin Lot (Alcohol Anhydrous + Erythromycin + Laureth 4)
  3. Stievamycin Forte Gel (Erythromycin + Tretinoin)
  4. Stievamycin Gel (Erythromycin + Tretinoin)
  5. T-Stat Lot (Alcohol Anhydrous + Erythromycin)
  6. T-Stat Pad-Lot (Alcohol Anhydrous + Erythromycin)
Chemical IUPAC Name (3R,4S,5S,6R,7R,9R,11R,12R,13S,14R)-6-[(2S,3R,4S,6R)-4-dimethylamino-3-hydroxy-6-methyloxan-2-yl]oxy-14-ethyl-7,12,13-trihydroxy-4-[(2R,4R,5S,6S)-5-hydroxy-4-methoxy-4,6-dimethyloxan-2-yl]oxy-3,5,7,9,11,13-hexamethyl-1-oxacyclotetradecane-2,10-dione
Chemical Formula C37H67NO13
Chemical Structure Structure
CAS Registry Number 114-07-8
InChI Identifier InChI=1/C37H67NO13/c1-14-25-37(10,45)30(41)20(4)27(39)18(2)16-35(8,44)32(51-34-28(40)24(38(11)12)15-19(3)47-34)21(5)29(22(6)33(43)49-25)50-26-17-36(9,46-13)31(42)23(7)48-26/h18-26,28-32,34,40-42,44-45H,14-17H2,1-13H3/t18-,19-,20+,21+,22-,23+,24+,25-,26+,28-,29+,30-,31+,32-,34+,35-,36-,37-/m1/s1
InChI Key ULGZDMOVFRHVEP-RWJQBGPGBH
KEGG Drug D00140 Link Image
KEGG Compound C01912 Link Image
PubChem Compound 12560 Link Image
PubChem Substance 5020 Link Image
ChEBI ID Not Available
PharmGKB ID PA449493 Link Image
HET ID ERY Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02237041 Link Image
RxList Link http://www.rxlist.com/cgi/generic/erithrom.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/ery1163.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Erythromycin Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 733.9268
Monoisotopic Molecular Weight 733.4612
State Solid
Melting Point 191 oC
Experimental Water Solubility Slightly soluble (1.44 mg/L) Source: PhysProp
Predicted Water Solubility 4.59e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3.06 [MCFARLAND,JW ET AL. (1997)] Source: PhysProp
Predicted LogP 2.37 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.20 Calculated using ALOGPS
Experimental Caco2 Permeability -5.43 [ADME Research, USCD]
pKa/Isoelectric Point 8.88
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)C(=O)[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)C(=O)C(C)C(O)C1(C)O
Drug Category
  • Anti-Bacterial Agents
  • Macrolides
ATC Codes
AHFS Codes
  • 08:12.12.04
  • 34:00.00
  • 52:04.04
Indication For use in the treatment of infections caused by susceptible strains of microorganisms in the following diseases: respiratory tract infections (upper and lower) of mild to moderate degree, pertussis (whooping cough), as adjunct to antitoxin in infections due to Corynebacterium diphtheriae, in the treatment of infections due to Corynebacterium minutissimum, intestinal amebiasis caused by Entamoeba histolytica, acute pelvic inflammatory disease caused by Neisseria gonorrhoeae, skin and soft tissue infections of mild to moderate severity caused by Streptococcus pyogenes and Staphylococcus aureus, primary syphilis caused by Treponema pallidum, infections caused by Chlamydia trachomatis, nongonococcal urethritis caused by Ureaplasma urealyticum, and Legionnaires' disease caused by Legionella pneumophila.
Pharmacology Erythromycin is produced by a strain of Streptomyces erythraeus and belongs to the macrolide group of antibiotics. After absorption, erythromycin diffuses readily into most body fluids. In the absence of meningeal inflammation, low concentrations are normally achieved in the spinal fluid, but the passage of the drug across the blood-brain barrier increases in meningitis. Erythromycin is excreted in breast milk. The drug crosses the placental barrier, but fetal plasma levels are low. Erythromycin is not removed by peritoneal dialysis or hemodialysis.
Mechanism of Action Erythromycin acts by penetrating the bacterial cell membrane and reversibly binding to the 50 S subunit of bacterial ribosomes or near the “P” or donor site so that binding of tRNA (transfer RNA) to the donor site is blocked. Translocation of peptides from the “A” or acceptor site to the “P” or donor site is prevented, and subsequent protein synthesis is inhibited. Erythromycin is effective only against actively dividing organisms. The exact mechanism by which erythmromycin reduces lesions of acne vulgaris is not fully known: however, the effect appears to be due in part to the antibacterial activity of the drug.
Absorption Orally administered erythromycin base and its salts are readily absorbed in the microbiologically active form. Topical application of the ophthalmic ointment to the eye may result in absorption into the cornea and aqueous humor.
Toxicity Symptoms of overdose include diarrhea, nausea, stomach cramps, and vomiting.
Protein Binding Erythromycin is largely bound to plasma proteins, and the freely dissociating bound fraction after administration of erythromycin base represents 90% of the total erythromycin absorbed.
Biotransformation Hepatic. Extensively metabolized - after oral administration, less than 5% of the administered dose can be recovered in the active form in the urine.
Half Life 1.5 hours
Dosage Forms
Form Route
Capsule, coated Oral
Liquid Dental
Liquid Oral
Ointment Ophthalmic
Powder Intravenous
Powder Oral
Powder, for solution Intravenous
Powder, for solution Oral
Powder, for suspension Oral
Suspension Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The macrolide increases anticoagulant effect
Alfentanil The macrolide increases the effect and toxicity of alfentanil
Alprazolam The macrolide increases the effect of the benzodiazepine
Aminophylline The macrolide increases the effect and toxicity of theophylline
Amiodarone Increased risk of cardiotoxicity and arrhythmias
Anisindione The macrolide increases anticoagulant effect
Aprepitant This CYP3A4 inhibitor increases effect and toxicity of aprepitant
Astemizole Increased risk of cardiotoxicity and arrhythmias
Atorvastatin The macrolide possibly increases the statin toxicity
Bretylium Increased risk of cardiotoxicity and arryhthmias
Bromocriptine Erythromycin increases serum levels of bromocriptine
Buspirone The macrolide increases the effect and toxicity of buspirone
Cabergoline Erythromycin increases serum levels and toxicity of cabergoline
Carbamazepine The macrolide increases the effect of carbamazepine
Cerivastatin The macrolide possibly increases the statin toxicity
Cilostazol Erythromycin increases the effect of cilostazol
Cinacalcet This macrolide increases the serum levels and toxicity of cinacalcet
Cisapride Increased risk of cardiotoxicity and arrhythmias
Citalopram Possible serotoninergic syndrome with this combination
Clozapine Erythromycin increases the effect of clozapine
Colchicine Severe colchicine toxicity can occur
Cyclosporine The macrolide increases the effect of cyclosporine
Diazepam The macrolide increases the effect of the benzodiazepine
Dicumarol The macrolide increases anticoagulant effect
Digoxin The macrolide increases the effect of digoxin in 10% of patients
Dihydroergotamine Possible ergotism and severe ischemia with this combination
Dihydroergotoxine Possible ergotism and severe ischemia with this combination
Disopyramide Increased risk of cardiotoxicity and arrhythmias
Divalproex sodium Erythromycin increases the effect of valproic acid
Docetaxel The agent increases the serum levels and toxicity of docetaxel
Dofetilide Increased risk of cardiotoxicity and arrhythmias
Dyphylline The macrolide increases the effect and toxicity of theophylline
Eletriptan The macrolide increases the effect and toxicity of eletriptan
Eplerenone This CYP3A4 inhibitor increases the effect and toxicity of eplerenone
Ergonovine Possible ergotism and severe ischemia with this combination
Ergotamine Possible ergotism and severe ischemia with this combination
Erlotinib This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Everolimus The macrolide increases everolimus levels/toxicity
Felodipine Erythromycin increases the effect of felodipine
Fluoxetine Possible serotoninergic syndrome with this combination
Gefitinib This CYP3A4 inhibitor increases levels/toxicity of gefitinib
Grepafloxacin Increased risk of cardiotoxicity and arrhythmias
Imatinib The macrolide increases levels of imatinib
Itraconazole The macrolide increases the effect and toxicity of itraconazole
Levofloxacin Increased risk of cardiotoxicity and arrhythmias
Lincomycin Possible antagonism of action with this combination
Lovastatin The macrolide possibly increases the statin toxicity
Mesoridazine Increased risk of cardiotoxicity and arrhythmias
Methylergonovine Possible ergotism and severe ischemia with this combination
Methylprednisolone The macrolide increases the effect of corticosteroid
Methysergide Possible ergotism and severe ischemia with this combination
Midazolam The macrolide increases the efect of the benzodiazepine
Moxifloxacin Increased risk of cardiotoxicity and arrhythmias
Oxtriphylline The macrolide increases the effect and toxicity of theophylline
Pimozide Increased risk of cardiotoxicity and arrhythmias
Quetiapine This macrolide increases the effect/toxicity of quetiapine
Quinidine Increased risk of cardiotoxicity and arrhythmias
Quinidine barbiturate Increased risk of cardiotoxicity and arrhythmias
Quinupristin This combination presents an increased risk of toxicity
Ranolazine Increased levels of ranolazine - risk of toxicity
Repaglinide This macrolide increases effect of repaglinide
Rifabutin The rifamycin decreases the effect of the macrolide
Rifampin The rifamycin decreases the effect of the macrolide
Ritonavir Increased toxicity of both agents
Sertraline Possible serotoninergic syndrome with this combination
Sibutramine Erythromycin increases the effect and toxicity of sibutramine
Sildenafil The macrolide increases the effect and toxicity of sildenafil
Simvastatin The macrolide possibly increases the statin toxicity
Sirolimus The macrolide increases sirolimus levels
Sotalol Increased risk of cardiotoxicity and arrhythmias
Sparfloxacin Increased risk of cardiotoxicity and arrhythmias
Tacrolimus Erythromycin increases the effect and toxicity of tacrolimus
Terfenadine Increased risk of cardiotoxicity and arrhythmias
Theophylline The macrolide increases the effect and toxicity of theophylline
Thioridazine Increased risk of cardiotoxicity and arrhythmias
Triazolam The macrolide increases the effect of the benzodiazepine
Vardenafil The macrolide increases the effect and toxicity of vardenafil
Verapamil Increased risk of cardiotoxicity and arrhythmias
Vinblastine Erythromycin increases vinblastine toxicity
Warfarin The macrolide increases anticoagulant effect
Zafirlukast Erythromycin decreases the effect of zafirlukast
Food Interactions
  • Avoid alcohol.
  • Take on empty stomach: 1 hour before or 2 hours after meals.
  • Take with a full glass of water Avoid taking with grapefruit juice.
Pathways
Name SMPDB Link KEGG Link
Erythromycin Pathway SMP00250 Link Image
General References
  1. Kanazawa S, Ohkubo T, Sugawara K: The effects of grapefruit juice on the pharmacokinetics of erythromycin. Eur J Clin Pharmacol. 2001 Jan-Feb;56(11):799-803. [PubMed Link Image]
  2. Ogwal S, Xide TU: Bioavailability and stability of erythromycin delayed release tablets. Afr Health Sci. 2001 Dec;1(2):90-6. [PubMed Link Image]
  3. Okudaira T, Kotegawa T, Imai H, Tsutsumi K, Nakano S, Ohashi K: Effect of the treatment period with erythromycin on cytochrome P450 3A activity in humans. J Clin Pharmacol. 2007 Jul;47(7):871-6. [PubMed Link Image]
  4. Wikipedia Link Image
  5. RxList Link Image
  6. PDRhealth Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
  2. Adenosine deaminase
Targets
  1. 23S rRNA
  2. 50S ribosomal protein L22
  3. 50S ribosomal protein L4
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Adenosine deaminase
Enzyme 2 Gene Name ADA
Enzyme 2 SwissProt ID P00813 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >Adenosine deaminase 
AQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDF
LAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAE
GDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAID
LAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYH
TLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFK
STLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQ
NL
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. Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F: Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature. 2001 Oct 25;413(6858):814-21. [PubMed Link Image]
  2. Garza-Ramos G, Xiong L, Zhong P, Mankin A: Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA. J Bacteriol. 2001 Dec;183(23):6898-907. [PubMed Link Image]
  3. Moazed D, Noller HF: Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie. 1987 Aug;69(8):879-84. [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. Davydova N, Streltsov V, Wilce M, Liljas A, Garber M: L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin. J Mol Biol. 2002 Sep 20;322(3):635-44. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Rolain JM, Raoult D: Prediction of resistance to erythromycin in the genus Rickettsia by mutations in L22 ribosomal protein. J Antimicrob Chemother. 2005 Aug;56(2):396-8. Epub 2005 Jul 4. [PubMed Link Image]
  5. Cagliero C, Mouline C, Cloeckaert A, Payot S: Synergy between efflux pump CmeABC and modifications in ribosomal proteins L4 and L22 in conferring macrolide resistance in Campylobacter jejuni and Campylobacter coli. Antimicrob Agents Chemother. 2006 Nov;50(11):3893-6. Epub 2006 Aug 28. [PubMed Link Image]
  6. 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. O'Connor M, Gregory ST, Dahlberg AE: Multiple defects in translation associated with altered ribosomal protein L4. Nucleic Acids Res. 2004 Oct 27;32(19):5750-6. Print 2004. [PubMed Link Image]
  3. 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]
  4. 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.