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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6YEO

Crystal structure of AmpC from E. coli with cyclic boronate 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
C0008800molecular_functionbeta-lactamase activity
C0016787molecular_functionhydrolase activity
C0017001biological_processantibiotic catabolic process
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0046677biological_processresponse to antibiotic
D0008800molecular_functionbeta-lactamase activity
D0016787molecular_functionhydrolase activity
D0017001biological_processantibiotic catabolic process
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue OK3 A 401
ChainResidue
ASER64
AGLY320
AASN346
AHOH518
AHOH536
ATYR150
AASN152
ATYR221
AASN289
ALYS315
ATHR316
AGLY317
AALA318
site_idAC2
Number of Residues5
Detailsbinding site for residue MPD A 402
ChainResidue
AARG232
ASER236
AILE243
AHOH581
AHOH620
site_idAC3
Number of Residues12
Detailsbinding site for residue EPE A 403
ChainResidue
AILE78
ALYS84
ALEU85
ASER86
ALEU254
ASER257
APRO304
AHOH511
AHOH671
CPRO303
CPRO306
CHOH526
site_idAC4
Number of Residues3
Detailsbinding site for residue NA A 404
ChainResidue
AHIS108
AHOH651
CHOH633
site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 405
ChainResidue
ATHR55
AGLN56
site_idAC6
Number of Residues3
Detailsbinding site for residue MPD B 402
ChainResidue
BASP242
DALA79
DARG80
site_idAC7
Number of Residues3
Detailsbinding site for residue GOL B 403
ChainResidue
BSER236
BHOH560
BHOH561
site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 404
ChainResidue
BGLN175
BILE189
BASN190
site_idAC9
Number of Residues1
Detailsbinding site for residue GOL C 402
ChainResidue
CASP242
site_idAD1
Number of Residues4
Detailsbinding site for residue GOL C 403
ChainResidue
CGLN52
CLYS197
CTYR199
CTRP201
site_idAD2
Number of Residues3
Detailsbinding site for residue GOL C 404
ChainResidue
CLEU182
CSER236
CILE243
site_idAD3
Number of Residues3
Detailsbinding site for residue MPD D 402
ChainResidue
DPRO140
DTRP142
DHOH501
site_idAD4
Number of Residues13
Detailsbinding site for residue EPE D 403
ChainResidue
BPRO304
BPRO306
BHOH592
DILE78
DLYS84
DLEU85
DSER86
DLEU254
DSER257
DPRO304
DHOH509
DHOH521
DHOH584
site_idAD5
Number of Residues18
Detailsbinding site for Di-peptide OK3 B 401 and SER B 64
ChainResidue
BLEU62
BGLY63
BVAL65
BSER66
BLYS67
BTYR150
BASN152
BALA220
BTYR221
BASN289
BLYS315
BTHR316
BGLY317
BALA318
BTHR319
BGLY320
BASN346
BHOH501
site_idAD6
Number of Residues20
Detailsbinding site for Di-peptide OK3 C 401 and SER C 64
ChainResidue
CGLY317
CALA318
CTHR319
CGLY320
CASN346
CHOH503
CHOH542
CLEU62
CGLY63
CVAL65
CSER66
CLYS67
CTYR150
CASN152
CARG204
CALA220
CTYR221
CASN289
CLYS315
CTHR316
site_idAD7
Number of Residues19
Detailsbinding site for Di-peptide OK3 D 401 and SER D 64
ChainResidue
DLEU62
DGLY63
DVAL65
DSER66
DLYS67
DTYR150
DASN152
DALA220
DTYR221
DASN289
DLYS315
DTHR316
DGLY317
DALA318
DGLY320
DASN346
DHOH504
DHOH534
DHOH537
Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67
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

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