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1A7T

METALLO-BETA-LACTAMASE WITH MES

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
AZN252
AHOH256

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 252
ChainResidue
AHOH256
AHOH257
AASP86
ACYS164
AHIS206
AZN251

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 255
ChainResidue
AASN38
AASP52
AASP86
AHOH258
AHOH266

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 251
ChainResidue
BHIS82
BHIS84
BHIS145
BZN252
BHOH256

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 252
ChainResidue
BASP86
BCYS164
BHIS206
BZN251
BHOH256
BHOH257

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 255
ChainResidue
BASN38
BASP52
BASP86
BHOH259
BHOH263

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 250
ChainResidue
ATRP32
AASP86
AHIS145
AGLY175
AASN176
AHIS206
AHOH257
AHOH329
BARG200

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES B 250
ChainResidue
BTRP32
BASP86
BHIS145
BGLY175
BASN176
BHOH257
BHOH282
BHOH342

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
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

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PDB entries from 2024-10-09

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