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4FH4

high-resolution structure of apo wt SHV-1 beta-lactamase

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 Residues21
DetailsBINDING SITE FOR RESIDUE MA4 A 301
ChainResidue
AARG93
AILE279
AALA280
AALA284
AGLU288
AMA4302
AHOH403
AHOH436
AHOH526
AHOH632
AHOH656
ALYS94
AHOH687
AHOH761
AILE95
AHIS96
AVAL224
APRO226
AALA248
AVAL261
AILE263

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MA4 A 302
ChainResidue
ASER26
AARG98
AASP101
AARG244
AASN276
AGLN277
AILE279
AALA280
AGLY281
AALA284
AMA4301
AHOH656
AHOH684
AHOH736
AHOH747
AHOH794
AHOH812
AHOH845

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 2024-07-24

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