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1CK3

N276D MUTANT OF ESCHERICHIA COLI TEM-1 BETA-LACTAMASE

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
APHE66-LEU81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER70

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU168

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS234

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

site_idMCSA1
Number of Residues6
DetailsM-CSA 2
ChainResidueDetails
ASER70electrostatic stabiliser
ALYS73hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER130activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU166activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS234electrostatic stabiliser
AALA237electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-01

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