Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MQO

Metallo-beta-lactamase BcII Cd substituted from Bacillus cereus at 1.35 angstroms resolution

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 Residues6
DetailsBINDING SITE FOR RESIDUE CD A 1
ChainResidue
ACD3
AHIS116
AHIS118
AASP120
AHIS196
ACIT300

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CD A 3
ChainResidue
AHIS118
AASP120
AHIS196
ACYS221
ACIT300
ACD1
ACD2
AHIS116

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 2
ChainResidue
ACD3
ACYS221
AHIS263
ACIT300
AHOH335

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 300
ChainResidue
ACD1
ACD2
ACD3
AHIS118
AASP120
AHIS196
ACYS221
AGLY232
AASN233
AHIS263
AHOH330
AHOH347
AHOH391

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADriGGiktlker.G
ChainResidueDetails
AILE113-GLY133

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: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:7588620, ECO:0000269|PubMed:9761898
ChainResidueDetails
AHIS116
AHIS118
AHIS196

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303
ChainResidueDetails
AASP120
ACYS221
AHIS263

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303
ChainResidueDetails
ALYS224

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:9761898
ChainResidueDetails
AASN233

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120
AASN233

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP120

site_idMCSA1
Number of Residues5
DetailsM-CSA 16
ChainResidueDetails
AHIS116metal ligand
AHIS118metal ligand
AASP120hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS196metal ligand
AASN233electrostatic stabiliser, hydrogen bond donor

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon