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4ZNB

METALLO-BETA-LACTAMASE (C181S MUTANT)

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 1
ChainResidue
AHIS99
AHIS101
AASP103
AHIS162
AHOH250

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 3
ChainResidue
AASN55
AASP69
AASP103
AHOH256

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BHIS99
BHIS101
BHIS162
BHOH250

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 3
ChainResidue
BASN55
BASP69
BASP103
BHOH253

site_idNAA
Number of Residues4
DetailsDEDUCED FROM THE COORDINATION. SODIUM WAS PRESENT IN THE CRYSTALLIZATION SOLUTION.
ChainResidue
AASP69
AASP103
AHOH256
AASN55

site_idNAB
Number of Residues4
DetailsDEDUCED FROM THE COORDINATION. SODIUM WAS PRESENT IN THE CRYSTALLIZATION SOLUTION.
ChainResidue
BASN55
BASP69
BASP103
BHOH253

site_idZNA
Number of Residues4
DetailsONLY THE ZN1 SITE OF THE BINUCLEAR ZINC CENTER IS OCCUPIED.
ChainResidue
AHIS99
AHIS101
AHIS162
AHOH250

site_idZNB
Number of Residues4
DetailsONLY THE ZN1 SITE OF THE BINUCLEAR ZINC CENTER IS OCCUPIED.
ChainResidue
BHIS99
BHIS101
BHIS162
BHOH250

Functional Information from PROSITE/UniProt
site_idPS00743
Number of Residues20
DetailsBETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqkk.G
ChainResidueDetails
AILE96-GLY115

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
AHIS99
AHIS101
AHIS162
BHIS99
BHIS101
BHIS162

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
AASP103
ASER181
AHIS223
BASP103
BSER181
BHIS223

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9545432
ChainResidueDetails
ALYS184
BLYS184

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12019104, ECO:0000269|PubMed:9545432, ECO:0000269|PubMed:9578564
ChainResidueDetails
AASN193
BASN193

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP103
AASN193

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP103
BASN193

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP103

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
BASP103

site_idMCSA1
Number of Residues8
DetailsM-CSA 15
ChainResidueDetails
AHIS99metal ligand
AHIS101metal ligand
AASP103metal ligand
AHIS162metal ligand
ASER181metal ligand
ALYS184electrostatic stabiliser, steric role
AASN193electrostatic stabiliser, hydrogen bond donor
AHIS223metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 15
ChainResidueDetails
BHIS99metal ligand
BHIS101metal ligand
BASP103metal ligand
BHIS162metal ligand
BSER181metal ligand
BLYS184electrostatic stabiliser, steric role
BASN193electrostatic stabiliser, hydrogen bond donor
BHIS223metal ligand

223166

PDB entries from 2024-07-31

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