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3SH7

Crystal structure of fluorophore-labeled beta-lactamase PenP

Replaces:  3KGM
Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
B0005886cellular_componentplasma membrane
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030655biological_processbeta-lactam antibiotic catabolic process
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BB0 A 2
ChainResidue
AASN104
AASN132
ACYS166
ALEU169
AALA237
AHOH460

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BB0 B 2
ChainResidue
BASN104
BCYS166
BLEU169

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVA
ChainResidueDetails
APHE47-ALA59

site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL
ChainResidueDetails
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70
BSER70

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU168
BGLU168

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS234
BLYS234

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PDB entries from 2024-07-17

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