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2BMI

METALLO-BETA-LACTAMASE

Replaces:  1BMI
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 271
ChainResidue
AHIS82
AHIS84
AHIS145
AZN272
AHOH276

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 271
ChainResidue
BHIS82
BHIS84
BHIS145
BZN272
BHOH278

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 272
ChainResidue
AASP86
ACYS164
AHIS206
AZN271
AHOH276
AHOH492

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 275
ChainResidue
AASN38
AASP52
AASP86
AHOH493
AHOH494

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 272
ChainResidue
BASP86
BCYS164
BHIS206
BZN271
BHOH278
BHOH474

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 275
ChainResidue
BASN38
BASP52
BASP86
BHOH279
BHOH475

site_idAS1
Number of Residues3
DetailsPROTEIN ZINC LIGANDS
ChainResidue
AHIS82
AHIS84
AHIS145

site_idAS2
Number of Residues3
DetailsPROTEIN ZINC LIGANDS
ChainResidue
AHIS206
ACYS164
AASP86

site_idBS1
Number of Residues3
DetailsPROTEIN ZINC LIGANDS
ChainResidue
BHIS82
BHIS84
BHIS145

site_idBS2
Number of Residues3
DetailsPROTEIN ZINC LIGANDS
ChainResidue
BHIS206
BCYS164
BASP86

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: BINDING => ECO:0000269|PubMed:10210203, ECO:0000269|PubMed:12019104, ECO:0000269|PubMed:8805566, ECO:0000269|PubMed:9416622, ECO:0000269|PubMed:9545432, ECO:0000269|PubMed:9578564, ECO:0000269|PubMed:9761816
ChainResidueDetails
AHIS82
AHIS84
AHIS145
BHIS82
BHIS84
BHIS145

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12019104, ECO:0000269|PubMed:8805566, ECO:0000269|PubMed:9416622, ECO:0000269|PubMed:9545432, ECO:0000269|PubMed:9578564, ECO:0000269|PubMed:9761816
ChainResidueDetails
AASP86
ACYS164
AHIS206
BASP86
BCYS164
BHIS206

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9545432
ChainResidueDetails
ALYS167
BLYS167

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12019104, ECO:0000269|PubMed:9545432, ECO:0000269|PubMed:9578564
ChainResidueDetails
AASN176
BASN176

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9578564, 9730812
ChainResidueDetails
AASP86
AASN176

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9578564, 9730812
ChainResidueDetails
BASP86
BASN176

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

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PDB entries from 2024-07-10

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