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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4KG5

Crystal Structure of AmpC beta-lactamase N152G Mutant in Complex with Cefotaxime

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 401
ChainResidue
BHIS186
BLYS290
site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PCZ B 402
ChainResidue
BGLY320
BASN346
BHOH526
BHOH544
BHOH546
BHOH578
BSER64
BVAL211
BTYR221
BASN289
BGLY317
BALA318
BTHR319
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
AHIS186
ALYS290
APO4402
CSER129
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AHIS186
AGLU195
ALYS197
AASN198
APO4401
AHOH614
site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 403
ChainResidue
ASER129
AARG133
CHIS186
site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PCZ A 404
ChainResidue
ASER64
AVAL211
ATYR221
AASN289
ALEU293
AGLY317
AALA318
ATHR319
AGLY320
AASN346
AHOH515
site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PCZ C 401
ChainResidue
CSER64
CLEU119
CVAL211
CTYR221
CASN289
CGLY317
CALA318
CGLY320
CHOH560
CHOH578
CHOH619
site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 D 401
ChainResidue
BARG133
CLYS290
DHIS186
DGLU195
site_idAC9
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PCZ D 402
ChainResidue
DSER64
DLEU119
DGLN120
DVAL211
DTYR221
DASN289
DGLY317
DALA318
DTHR319
DGLY320
DASN343
DASN346
DHOH507
DHOH542
DHOH584
Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
BPHE60-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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