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3D4F

SHV-1 beta-lactamase complex with LN1-255

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MA4 A 400
ChainResidue
AARG93
AHOH658
AHOH686
AHOH767
AHOH797
AHOH798
AILE95
AHIS96
AARG98
APRO226
AALA280
AALA284
AGLU288
AHOH614

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MA4 A 401
ChainResidue
AARG244
AILE279

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LN1 A 601
ChainResidue
ASER70
ATYR105
ASER130
AASN132
ALEU220
ALYS234
ATHR235
AGLY236
AALA237
AARG244
AASN276
AHOH690
AHOH736
AHOH794

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1btl
ChainResidueDetails
AGLU166
ALYS73
ASER130
ASER70

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PDB entries from 2024-07-10

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