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2UYX

metallo-beta-lactamase (1BC2) single point mutant D120S

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A1292
ChainResidue
AHIS118
AHOH2280
AHOH2281
ASER120
AHIS196
AGOL1293
AZN1296
AZN1297
AHOH2277
AHOH2278
AHOH2279

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A1293
ChainResidue
AHIS118
AALA119
ASER120
ACYS221
AGOL1292
AZN1296
AZN1297
AHOH2277
AHOH2279
AHOH2280
AHOH2281

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1294
ChainResidue
AALA117
AHIS118
AASN149
ATHR197
AASP199
AASP236

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1295
ChainResidue
AGLU97
AGLU130
AARG131
AHOH2077

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A1296
ChainResidue
AHIS116
AHIS118
AHIS196
AGOL1292
AGOL1293
AHOH2281

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A1297
ChainResidue
ACYS221
AHIS263
AGOL1292
AGOL1293
AHOH2280
AHOH2283

Functional Information from PROSITE/UniProt
site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK
ChainResidueDetails
APRO209-LYS224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
ASER120

site_idMCSA1
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
ASER120hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS196metal ligand
AASN233electrostatic stabiliser, hydrogen bond donor

247947

PDB entries from 2026-01-21

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