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1KR3

Crystal Structure of the Metallo beta-Lactamase from Bacteroides fragilis (CfiA) in Complex with the Tricyclic Inhibitor SB-236050.

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS99
AHIS101
AHIS162
AZN302

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AASP103
ACYS181
AHIS223
AZN301
A113602

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BHIS99
BHIS101
BHIS162
B113601
BHOH616

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BASP103
BCYS181
BHIS223
B113601
BHOH616

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
ATYR40
AASN55
AASP69
ATHR70
AASP103
AHOH616

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BSER54
BASN55
BTHR70
BASP103

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 113 B 601
ChainResidue
BHIS162
BCYS181
BLYS184
BSER190
BASN193
BHIS223
BZN401
BZN402
BHOH616

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 113 A 602
ChainResidue
AILE46
AHIS162
ACYS181
ALYS184
AASN193
AHIS223
AZN302

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

site_idPS00744
Number of Residues13
DetailsBETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PtenILfGgCMLK
ChainResidueDetails
APRO172-LYS184

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
ACYS181
AHIS223
BASP103
BCYS181
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
ACYS181metal 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
BCYS181metal ligand
BLYS184electrostatic stabiliser, steric role
BASN193electrostatic stabiliser, hydrogen bond donor
BHIS223metal ligand

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PDB entries from 2024-07-24

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