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4GKU

Crystal structure of beta lactamase in PET-15B

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030655biological_processbeta-lactam antibiotic catabolic process
A0046677biological_processresponse to antibiotic
Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
ChainResidueDetails
APHE64-LEU79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 2
ChainResidueDetails
ASER68electrostatic stabiliser
ALYS71hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER128activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU164activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS232electrostatic stabiliser
AALA235electrostatic stabiliser, hydrogen bond donor

246704

PDB entries from 2025-12-24

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