Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EUZ

GLUTAMATE DEHYDROGENASE FROM THERMOCOCCUS PROFUNDUS IN THE UNLIGATED STATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
A	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
A	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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
B	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
B	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
B	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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
C	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
C	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
C	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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
D	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
D	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
D	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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
E	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
E	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
E	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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
F	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
F	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
F	0004354	molecular_function	glutamate dehydrogenase (NADP+) activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 600

Chain	Residue
A	SER24
A	GLU25
A	LYS419

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 601

Chain	Residue
A	LYS69
A	GLY70
A	MET90
A	ALA143
A	VAL348
A	SER351

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	THR191
A	ASN222
A	ALA223

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 603

Chain	Residue
A	ARG331
A	HIS388

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 604

Chain	Residue
A	ASP413
C	PRO178
C	LEU179

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 605

Chain	Residue
A	ASP244
A	SER245
A	LYS264

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 606

Chain	Residue
B	PRO178
B	LEU179
B	ARG187

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 607

Chain	Residue
B	THR191
B	ASN222
B	ALA223

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 608

Chain	Residue
B	ASP244
B	SER245
B	LYS264

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 609

Chain	Residue
C	SER245
C	LYS264

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 610

Chain	Residue
D	PRO178
D	LEU179
E	ASP413

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 611

Chain	Residue
E	SER24
E	GLU25
E	LYS419

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 E 612

Chain	Residue
E	PRO178
E	LEU179

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 613

Chain	Residue
E	SER245
E	ARG246
E	GLY247
E	THR280
E	ASN281

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 614

Chain	Residue
E	ASP244
E	SER245
E	LYS264

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 F 615

Chain	Residue
F	PRO178
F	LEU179

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 616

Chain	Residue
F	ASP244
F	SER245
F	LYS264

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU99-PRO112

Functional Information from SwissProt/UniProt

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

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
A	ASP145
A	LYS105

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
B	ASP145
B	LYS105

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
C	ASP145
C	LYS105

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
D	ASP145
D	LYS105

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
E	ASP145
E	LYS105

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1hrd

Chain	Residue	Details
F	ASP145
F	LYS105

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)