4ZJ2

Crystal Structure of p-acrylamido-phenylalanine modified TEM1 beta-lactamase from Escherichia coli :E166N mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008800	molecular_function	beta-lactamase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030655	biological_process	beta-lactam antibiotic catabolic process
A	0046677	biological_process	response to antibiotic

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Acyl-ester intermediate

Chain	Residue	Details
A	4OV70

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	GLU168

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS234

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 2

Chain	Residue	Details
A	4OV70	electrostatic stabiliser
A	LYS73	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	SER130	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN166	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS234	electrostatic stabiliser
A	ALA237	electrostatic stabiliser, hydrogen bond donor

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