Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6XFS

Class C beta-lactamase from Escherichia coli in complex with Tazobactam

Replaces:  6WA7
Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
C0030288cellular_componentouter membrane-bounded periplasmic space
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
D0030288cellular_componentouter membrane-bounded periplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue TBE A 501
ChainResidue
ASER91
AGLN147
ATYR248
AALA345
ATHR346

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 502
ChainResidue
AGLU299
ALYS342
ATHR343

site_idAC3
Number of Residues1
Detailsbinding site for residue EDO A 503
ChainResidue
APRO192

site_idAC4
Number of Residues8
Detailsbinding site for residue PGE B 502
ChainResidue
BLYS326
BPRO327
BTHR329
BHOH601
CPRO115
CGLY130
CTHR132
CHIS135

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 503
ChainResidue
BSER314
BHIS341
BLYS342
BTHR343
BHOH615

site_idAC6
Number of Residues6
Detailsbinding site for residue PEG C 401
ChainResidue
CTYR177
CGLU299
CSER314
CHIS341
CLYS342
CTHR343

site_idAC7
Number of Residues8
Detailsbinding site for residue PGE D 502
ChainResidue
DSER91
DGLU299
DSER314
DASN316
DALA319
DTHR343
DASN373
DTBE501

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO D 503
ChainResidue
DASN36
DHIS40

site_idAC9
Number of Residues15
Detailsbinding site for Di-peptide TBE B 501 and SER B 91
ChainResidue
BLEU89
BGLY90
BVAL92
BSER93
BLYS94
BGLN147
BTYR177
BALA247
BTYR248
BLYS342
BTHR343
BGLY344
BALA345
BTHR346
BGLY347

site_idAD1
Number of Residues16
Detailsbinding site for Di-peptide TBE C 402 and SER C 91
ChainResidue
CLEU89
CGLY90
CVAL92
CSER93
CLYS94
CGLN147
CTYR177
CASN179
CALA247
CTYR248
CLYS342
CTHR343
CGLY344
CALA345
CTHR346
CGLY347

site_idAD2
Number of Residues16
Detailsbinding site for Di-peptide TBE D 501 and SER D 91
ChainResidue
DLEU89
DGLY90
DVAL92
DSER93
DLYS94
DGLN147
DTYR177
DALA247
DTYR248
DLYS342
DTHR343
DGLY344
DALA345
DTHR346
DGLY347
DPGE502

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE87-LYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10102","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11478888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35486701","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6795623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9819201","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

PDB statisticsPDBj update infoContact PDBjnumon