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1BVT

METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9

Replaces:  1BME
Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 229
ChainResidue
AASP90
ACYS168
AHIS210
ABCT230

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BCT A 230
ChainResidue
AZN229
AHOH357
AHOH516
AHIS149
ACYS168
AASN180
AHIS210

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 228
ChainResidue
AHIS86
AHIS88
AHIS149
AHOH516

site_idZN1
Number of Residues1
DetailsWATER 301 LINK TO ZN 228 , THIS SITE IS THE CATALYTIC SITE
ChainResidue
AASP90

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADriGGiktlker.G
ChainResidueDetails
AILE83-GLY102

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK
ChainResidueDetails
APRO159-LYS171

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 Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP90
AASN180

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP90

site_idMCSA1
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
AHIS86metal ligand
AHIS88metal ligand
AASP90hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS149metal ligand
AASN180electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-10-29

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