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

3MKF

SHV-1 beta-lactamase complex with GB0301

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CZ7 A 1
ChainResidue
AMET69
AGLU240
AHOH354
AHOH372
ASER70
ATYR105
AASN132
AGLU166
ATHR167
AASN170
AGLY236
AALA237

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MA4 A 600
ChainResidue
AARG93
ALYS94
AILE95
AHIS96
AVAL224
APRO226
AVAL261
AILE263
AALA280
AALA284
AGLU288
AHOH327
AHOH357
AHOH374
AHOH435

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MA4 A 601
ChainResidue
AARG244
AASN276

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvvlCGAVL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; acyl-ester intermediate => ECO:0000250|UniProtKB:A0A5R8T042, ECO:0000255|PROSITE-ProRule:PRU10101
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU168

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A5R8T042
ChainResidueDetails
ALYS73
ASER130
AGLU166

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon