Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3K92

Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
A	0005515	molecular_function	protein binding
A	0006520	biological_process	amino acid metabolic process
A	0006538	biological_process	L-glutamate catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A	0055114	biological_process	obsolete oxidation-reduction process
B	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
B	0005515	molecular_function	protein binding
B	0006520	biological_process	amino acid metabolic process
B	0006538	biological_process	L-glutamate catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B	0055114	biological_process	obsolete oxidation-reduction process
C	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
C	0005515	molecular_function	protein binding
C	0006520	biological_process	amino acid metabolic process
C	0006538	biological_process	L-glutamate catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C	0055114	biological_process	obsolete oxidation-reduction process
D	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
D	0005515	molecular_function	protein binding
D	0006520	biological_process	amino acid metabolic process
D	0006538	biological_process	L-glutamate catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D	0055114	biological_process	obsolete oxidation-reduction process
E	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
E	0005515	molecular_function	protein binding
E	0006520	biological_process	amino acid metabolic process
E	0006538	biological_process	L-glutamate catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E	0055114	biological_process	obsolete oxidation-reduction process
F	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
F	0005515	molecular_function	protein binding
F	0006520	biological_process	amino acid metabolic process
F	0006538	biological_process	L-glutamate catabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F	0055114	biological_process	obsolete oxidation-reduction process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 425

Chain	Residue
A	LEU131
A	ASN160
A	GLN162

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 425

Chain	Residue
C	LEU131
C	ASN160

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG D 425

Chain	Residue
D	ASN160

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG E 425

Chain	Residue
E	LEU131
E	ASN160

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG F 425

Chain	Residue
F	GLN162
F	ILE163
F	ASN160

Functional Information from PROSITE/UniProt

site_id	PS00074
Number of Residues	14
Details	GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGiicDP

Chain	Residue	Details
A	LEU110-PRO123

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details