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3MXS

SHV-1 beta-lactamase complex with compound 2

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 Residues13
DetailsBINDING SITE FOR RESIDUE CZ9 A 1
ChainResidue
AMET69
AGLY238
AGLU240
AGLN277
AHOH345
ASER70
ATYR105
AASN132
AGLU166
ATHR167
AASN170
AGLY236
AALA237

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MA4 A 400
ChainResidue
AHOH7
AARG93
AHIS96
AVAL224
APRO226
AALA248
AILE263
AILE279
AALA280
AALA284
AGLU288
AHOH302
AHOH412
AHOH415
AHOH453
AHOH472
AHOH513

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MA4 A 401
ChainResidue
AARG244
AASN276
AILE279

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

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PDB entries from 2024-07-10

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