3AGF

Crystal structure of Bacillus glutaminase in the presence of 4.3M NaCl

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004359	molecular_function	glutaminase activity
A	0006537	biological_process	glutamate biosynthetic process
A	0006541	biological_process	glutamine metabolic process
A	0006543	biological_process	L-glutamine catabolic process
A	0016787	molecular_function	hydrolase activity
B	0004359	molecular_function	glutaminase activity
B	0006537	biological_process	glutamate biosynthetic process
B	0006541	biological_process	glutamine metabolic process
B	0006543	biological_process	L-glutamine catabolic process
B	0016787	molecular_function	hydrolase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 301

Chain	Residue	Details
A	SER74	activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	LYS77	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR253	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	VAL271	electrostatic stabiliser, hydrogen bond donor

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 301

Chain	Residue	Details
B	SER74	activator, covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
B	LYS77	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	TYR201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	TYR253	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	VAL271	electrostatic stabiliser, hydrogen bond donor

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