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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:05
Primary Accession Number DB01212
Secondary Accession Number
  • APRD00395
Name Ceftriaxone
Drug Type
  • Approved
  • Small Molecule
Description A broad-spectrum cephalosporin antibiotic with a very long half-life and high penetrability to meninges, eyes and inner ears. [PubChem]
Synonyms
  1. Cefatriaxone
  2. Ceftriaxona [INN-Spanish]
  3. Ceftriaxonum [INN-Latin]
  4. Ceftriazone
Brand Names
  1. Biotrakson
  2. Rocephine
Brand Mixtures Not Available
Chemical IUPAC Name (6R,7R)-7-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-methoxyiminoacetyl]amino]-3-[(2-methyl-5,6-dioxo-1H-1,2,4-triazin-3-yl)sulfanylmethyl]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Chemical Formula C18H18N8O7S3
Chemical Structure Structure
CAS Registry Number 73384-59-5
InChI Identifier InChI=1/C18H18N8O7S3/c1-25-18(22-12(28)13(29)23-25)36-4-6-3-34-15-9(14(30)26(15)10(6)16(31)32)21-11(27)8(24-33-2)7-5-35-17(19)20-7/h5,9,15H,3-4H2,1-2H3,(H2,19,20)(H,21,27)(H,23,29)(H,31,32)/b24-8+/t9-,15-/m1/s1/f/h21,23,31H,19H2
InChI Key VAAUVRVFOQPIGI-QHUIQDKHDX
KEGG Drug Not Available
KEGG Compound C06683 Link Image
PubChem Compound 5361919 Link Image
PubChem Substance 189949 Link Image
ChEBI ID Not Available
PharmGKB ID PA448866 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00657409 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/ceftriax.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Ceftriaxone Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference M. Montavon, R. Reiner, Brit. pat. Appl. 2,022,090; eidem, U.S. pat. 4,327,210 (1979, 1982 both to Hoffmann-La Roche)
Average Molecular Weight 554.5800
Monoisotopic Molecular Weight 554.0461
State Solid
Melting Point >155 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.05e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -1.7 Source: PhysProp
Predicted LogP -0.00 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.72 Calculated using ALOGPS
Experimental Caco2 Permeability -6.88 [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 Not Available
Isomeric SMILES CO\N=C(C(=O)N[C@H]1[C@H]2SCC(CSC3=NC(=O)C(=O)NN3C)=C(N2C1=O)C(O)=O)/C1=CSC(N)=N1
Canonical SMILES CON=C(C(=O)NC1C2SCC(CSC3=NC(=O)C(=O)NN3C)=C(N2C1=O)C(O)=O)C1=CSC(N)=N1
Drug Category
  • Anti-Bacterial Agents
  • Cephalosporins
ATC Codes
AHFS Codes
  • 08:12.06.12
Indication For the treatment of the infections (respiratory, skin, soft tissue, UTI, ENT) caused by S. pneumoniae, H. influenzae, staphylococci, S. pyogenes (group A beta-hemolytic streptococci), E. coli, P. mirabilis, Klebsiella sp, coagulase-negative staph
Pharmacology Ceftriaxone is a cephalosporin/cephamycin beta-lactam antibiotic used in the treatment of bacterial infections caused by susceptible, usually gram-positive, organisms. Ceftriaxone has in vitro activity against gram-positive and gram-negative aerobic and anaerobic bacteria. The bactericidal activity of Ceftriaxone results from the inhibition of cell wall synthesis and is mediated through Ceftriaxone binding to penicillin binding proteins (PBPs). Ceftriaxone is stable against hydrolysis by a variety of beta-lactamases, including penicillinases, and cephalosporinases and extended spectrum beta-lactamases.
Mechanism of Action Ceftriaxone works by inhibiting the mucopeptide synthesis in the bacterial cell wall. The beta-lactam moiety of Ceftriaxone binds to carboxypeptidases, endopeptidases, and transpeptidases in the bacterial cytoplasmic membrane. These enzymes are involved in cell-wall synthesis and cell division. By binding to these enzymes, Ceftriaxone results in the formation of of defective cell walls and cell death.
Absorption Not Available
Toxicity Not Available
Protein Binding 95%
Biotransformation Not Available
Half Life 5.8-8.7 hours
Dosage Forms
Form Route
Powder, for solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The cephalosporin increases the anticoagulant effect
Amikacin Increased risk of nephrotoxicity
Anisindione The cephalosporin increases the anticoagulant effect
Dicumarol The cephalosporin increases the anticoagulant effect
Gentamicin Increased risk of nephrotoxicity
Kanamycin Increased risk of nephrotoxicity
Neomycin Increased risk of nephrotoxicity
Netilmicin Increased risk of nephrotoxicity
Streptomycin Increased risk of nephrotoxicity
Tobramycin Increased risk of nephrotoxicity
Warfarin The cephalosporin increases the anticoagulant effect
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Gamma-glutamyltranspeptidase
Drug Target 1 [top]
Target 1 ID 739
Target 1 Name Gamma-glutamyltranspeptidase
Target 1 Synonyms
  1. EC 2.3.2.2
  2. Gamma-glutamyltranspeptidase precursor
Target 1 Gene Name ggt
Target 1 Protein Sequence >Gamma-glutamyltranspeptidase precursor 
MIKPTFLRRVAIAALLSGSCFSAAAAPPAPPVSYGVEEDVFHPVRAKQGMVASVDATATQ
VGVDILKEGGNAVDAAVAVGYALAVTHPQAGNLGGGGFMLIRSKNGNTTAIDFREMAPAK
ATRDMFLDDQGNPDSKKSLTSHLASGTPGTVAGFSLALDKYGTMPLNKVVQPAFKLARDG
FIVNDALADDLKTYGSEVLPNHENSKAIFWKEGEPLKKGDTLVQANLAKSLEMIAENGPD
EFYKGTIAEQIAQEMQKNGGLITKEDLAAYKAVERTPISGDYRGYQVYSMPPPSSGGIHI
VQILNILENFDMKKYGFGSADAMQIMAEAEKYAYADRSEYLGDPDFVKVPWQALTNKAYA
KSIADQIDINKAKPSSEIRPGKLAPYESNQTTHYSVVDKDGNAVAVTYTLNTTFGTGIVA
GESGILLNNQMDDFSAKPGVPNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTG
SPGGSRIITTVLQMVVNSIDYGLNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAK
GQKVALKEAMGSTQSIMVGPDGELYGASDPRSVDDLTAGY
Target 1 Number of Residues 589
Target 1 Molecular Weight 61768
Target 1 Theoretical pI 5.26
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring amino-acyl groups
gamma-glutamyltransferase activity
Process
Not Available
Component
Not Available
Target 1 General Function Amino acid transport and metabolism
Target 1 Specific Function Not Available
Target 1 Pathways
Name SMPDB Link KEGG Link
Cyanoamino acid metabolism map00460 Link Image
Glutathione metabolism SMP00015 Link Image map00480 Link Image
Prostaglandin and leukotriene metabolism map00590 Link Image
Selenoamino acid metabolism SMP00029 Link Image map00450 Link Image
Taurine and hypotaurine metabolism SMP00021 Link Image map00430 Link Image
Target 1 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-25
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 146133 Link Image
Target 1 UniProtKB/Swiss-Prot ID P18956 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GGT_ECOLI Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Periplasm
Target 1 Gene Sequence >1743 bp 
ATGATAAAACCGACGTTTTTACGCCGGGTGGCCATTGCTGCTCTGCTCTCAGGAAGTTGT
TTTAGCGCCGCCGCCGCGCCTCCTGCGCCGCCCGTCTCGTATGGTGTGGAGGAAGATGTC
TTCCACCCGGTACGCGCGAAACAGGGAATGGTAGCGTCTGTGGACGCCACTGCCACTCAG
GTGGGGGTGGATATTCTCAAGGAGGGCGGGAATGCCGTTGATGCCGCCGTGGCGGTGGGC
TACGCGCTGGCGGTAACGCATCCGCAGGCAGGGAATCTGGGCGGTGGTGGTTTTATGTTA
ATCCGCTCGAAAAATGGCAATACCACGGCTATCGATTTCCGCGAAATGGCACCCGCCAAA
GCGACCCGCGATATGTTCCTCGATGATCAGGGCAACCCGGACAGCAAAAAATCACTCACT
TCGCATCTGGCTTCCGGCACACCGGGTACGGTAGCAGGTTTCTCGCTGGCGCTGGATAAA
TACGGCACCATGCCGCTGAACAAAGTCGTGCAGCCCGCGTTTAAACTGGCACGCGATGGT
TTTATCGTTAACGACGCGCTGGCTGACGATCTCAAAACCTACGGTAGCGAAGTGTTGCCG
AATCACGAAAACAGTAAAGCTATCTTCTGGAAAGAGGGCGAGCCGCTGAAAAAGGGCGAC
ACGCTGGTGCAGGCGAACCTGGCAAAGAGCCTGGAGATGATTGCTGAAAACGGCCCGGAC
GAATTCTATAAAGGCACGATTGCGGAACAGATCGCCCAGGAGATGCAGAAAAACGGTGGC
TTGATCACTAAAGAAGATTTAGCAGCCTATAAAGCGGTCGAACGCACTCCGATAAGCGGC
GATTATCGCGGGTATCAGGTTTACTCCATGCCACCGCCATCCTCCGGCGGGATCCATATC
GTACAAATCCTCAATATTCTGGAAAACTTCGATATGAAGAAATACGGCTTTGGCAGCGCC
GATGCGATGCAAATCATGGCAGAAGCGGAGAAATACGCCTACGCCGACCGCTCGGAATAT
CTTGGCGACCCGGATTTTGTCAAAGTACCGTGGCAGGCGCTGACCAATAAAGCCTATGCC
AAATCTATTGCCGATCAAATTGATATCAATAAAGCGAAGCCATCCAGCGAAATTCGCCCC
GGCAAGCTTGCGCCTTATGAGAGTAATCAAACTACCCATTACTCAGTGGTGGATAAAGAT
GGTAACGCGGTGGCGGTGACCTATACGCTGAACACCACCTTCGGTACGGGCATTGTCGCG
GGCGAGAGCGGTATTCTGCTTAATAACCAGATGGATGATTTCTCCGCCAAACCGGGCGTA
CCGAACGTTTACGGGCTGGTGGGCGGTGATGCCAACGCCGTCGGGCCGAACAAACGCCCG
CTGTCGTCGATGTCGCCGACCATTGTGGTGAAAGACGGTAAAACCTGGCTGGTTACCGGT
AGCCCAGGCGGTAGCCGGATCATCACTACAGTGCTGCAAATGGTGGTGAATAGCATCGAT
TATGGCTTGAACGTCGCCGAAGCGACCAATGCGCCGCGTTTCCACCATCAGTGGTTGCCG
GACGAGCTGCGTGTCGAAAAAGGGTTTAGCCCGGATACGCTCAAGCTGCTGGAAGCAAAA
GGTCAGAAAGTGGCGCTGAAAGAGGCGATGGGCAGTACACAAAGCATTATGGTTGGGCCG
GACGGTGAGTTGTACGGCGCATCCGACCCGCGCTCGGTGGATGATTTAACGGCGGGGTAC
TAA
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. Hashimoto W, Suzuki H, Nohara S, Kumagai H: Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits. Biochem Biophys Res Commun. 1992 Nov 30;189(1):173-8. [PubMed Link Image]
  2. Suzuki H, Kumagai H, Echigo T, Tochikura T: DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt. J Bacteriol. 1989 Sep;171(9):5169-72. [PubMed Link Image]
  3. Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
Target 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]

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.