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1A8T

METALLO-BETA-LACTAMASE IN COMPLEX WITH L-159,061

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
B0008270molecular_functionzinc ion binding
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 251
ChainResidue
AHIS82
AHIS84
AHIS145
A061250
AZN252

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 252
ChainResidue
A061250
AZN251
AASP86
AHIS145
ACYS164
AHIS206

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 251
ChainResidue
BHIS82
BHIS84
BHIS145
BZN252

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 252
ChainResidue
BASP86
BHIS145
BCYS164
BHIS206
BZN251

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 061 A 250
ChainResidue
AILE29
ATRP32
AVAL35
AHIS145
ACYS164
AASP168
AGLY175
AASN176
AHIS206
AGLY207
AASN208
AZN251
AZN252
AHOH282
AHOH315

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqrk.G
ChainResidueDetails
AILE79-GLY98

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK
ChainResidueDetails
APRO155-LYS167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10210203","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP86
AASN176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP86
BASN176

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP86

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP86

site_idMCSA1
Number of Residues8
DetailsM-CSA 15
ChainResidueDetails
AHIS82metal ligand
AHIS84metal ligand
AASP86metal ligand
AHIS145metal ligand
ACYS164metal ligand
ALYS167electrostatic stabiliser, steric role
AASN176electrostatic stabiliser, hydrogen bond donor
AHIS206metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 15
ChainResidueDetails
BHIS82metal ligand
BHIS84metal ligand
BASP86metal ligand
BHIS145metal ligand
BCYS164metal ligand
BLYS167electrostatic stabiliser, steric role
BASN176electrostatic stabiliser, hydrogen bond donor
BHIS206metal ligand

240971

PDB entries from 2025-08-27

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