Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6DHM

Bovine glutamate dehydrogenase complexed with zinc

Replaces: 3MVQReplaces: 1CH6Replaces: 1HWXReplaces: 3MW9

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
A	0005525	molecular_function	GTP binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005783	cellular_component	endoplasmic reticulum
A	0006520	biological_process	amino acid metabolic process
A	0006538	biological_process	L-glutamate catabolic process
A	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
A	0072350	biological_process	tricarboxylic acid metabolic process
B	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0005783	cellular_component	endoplasmic reticulum
B	0006520	biological_process	amino acid metabolic process
B	0006538	biological_process	L-glutamate catabolic process
B	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
B	0072350	biological_process	tricarboxylic acid metabolic process
C	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
C	0005525	molecular_function	GTP binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005783	cellular_component	endoplasmic reticulum
C	0006520	biological_process	amino acid metabolic process
C	0006538	biological_process	L-glutamate catabolic process
C	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
C	0072350	biological_process	tricarboxylic acid metabolic process
D	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
D	0005525	molecular_function	GTP binding
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0005783	cellular_component	endoplasmic reticulum
D	0006520	biological_process	amino acid metabolic process
D	0006538	biological_process	L-glutamate catabolic process
D	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
D	0072350	biological_process	tricarboxylic acid metabolic process
E	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
E	0005525	molecular_function	GTP binding
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0005783	cellular_component	endoplasmic reticulum
E	0006520	biological_process	amino acid metabolic process
E	0006538	biological_process	L-glutamate catabolic process
E	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
E	0072350	biological_process	tricarboxylic acid metabolic process
F	0000166	molecular_function	nucleotide binding
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	0005524	molecular_function	ATP binding
F	0005525	molecular_function	GTP binding
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0005783	cellular_component	endoplasmic reticulum
F	0006520	biological_process	amino acid metabolic process
F	0006538	biological_process	L-glutamate catabolic process
F	0006541	biological_process	glutamine metabolic 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	0042802	molecular_function	identical protein binding
F	0072350	biological_process	tricarboxylic acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue GLU A 601

Chain	Residue
A	LYS90
A	ASN349
A	VAL378
A	SER381
A	NDP602
A	GLY92
A	MET111
A	LYS114
A	LYS126
A	ALA166
A	PRO167
A	ASP168
A	ARG211

site_id	AC2
Number of Residues	19
Details	binding site for residue NDP A 602

Chain	Residue
A	ARG94
A	ASP168
A	MET169
A	SER170
A	ARG211
A	GLN250
A	GLY251
A	PHE252
A	GLY253
A	ASN254
A	VAL255
A	GLU275
A	SER276
A	ALA326
A	GLY347
A	ALA348
A	ASN349
A	ASN374
A	GLU601

site_id	AC3
Number of Residues	13
Details	binding site for residue GTP A 603

Chain	Residue
A	HIS209
A	GLY210
A	SER213
A	ARG217
A	HIS258
A	ARG261
A	TYR262
A	ARG265
A	LYS289
A	GLU292
A	LYS446
A	HIS450
A	ZN605

site_id	AC4
Number of Residues	2
Details	binding site for residue ZN A 604

Chain	Residue
A	GLU151
D	HIS57

site_id	AC5
Number of Residues	3
Details	binding site for residue ZN A 605

Chain	Residue
A	HIS209
A	HIS450
A	GTP603

site_id	AC6
Number of Residues	14
Details	binding site for residue GLU B 601

Chain	Residue
B	LYS90
B	GLY91
B	GLY92
B	MET111
B	LYS114
B	LYS126
B	ALA166
B	PRO167
B	ASP168
B	ARG211
B	ASN349
B	VAL378
B	SER381
B	NDP602

site_id	AC7
Number of Residues	20
Details	binding site for residue NDP B 602

Chain	Residue
B	ARG94
B	ASP168
B	MET169
B	SER170
B	ARG211
B	THR215
B	GLY251
B	PHE252
B	GLY253
B	ASN254
B	VAL255
B	GLU275
B	SER276
B	ALA325
B	ALA326
B	GLN330
B	ALA348
B	ASN349
B	ASN374
B	GLU601

site_id	AC8
Number of Residues	13
Details	binding site for residue GTP B 603

Chain	Residue
B	HIS209
B	GLY210
B	SER213
B	ARG217
B	HIS258
B	ARG261
B	TYR262
B	ARG265
B	LYS289
B	GLU292
B	LYS446
B	HIS450
B	ZN605

site_id	AC9
Number of Residues	2
Details	binding site for residue ZN B 604

Chain	Residue
B	GLU151
E	HIS57

site_id	AD1
Number of Residues	3
Details	binding site for residue ZN B 605

Chain	Residue
B	HIS209
B	HIS450
B	GTP603

site_id	AD2
Number of Residues	14
Details	binding site for residue GLU C 601

Chain	Residue
C	LYS90
C	GLY91
C	GLY92
C	MET111
C	LYS114
C	LYS126
C	ALA166
C	PRO167
C	ASP168
C	ARG211
C	ASN349
C	VAL378
C	SER381
C	NDP602

site_id	AD3
Number of Residues	22
Details	binding site for residue NDP C 602

Chain	Residue
C	ARG94
C	ASP168
C	MET169
C	SER170
C	ARG211
C	THR215
C	GLN250
C	GLY251
C	PHE252
C	GLY253
C	ASN254
C	VAL255
C	GLU275
C	SER276
C	ALA325
C	ALA326
C	SER327
C	GLN330
C	GLY347
C	ASN349
C	ASN374
C	GLU601

site_id	AD4
Number of Residues	12
Details	binding site for residue GTP C 603

Chain	Residue
C	HIS209
C	GLY210
C	SER213
C	ARG217
C	HIS258
C	ARG261
C	TYR262
C	ARG265
C	LYS289
C	GLU292
C	HIS450
C	ZN605

site_id	AD5
Number of Residues	3
Details	binding site for residue ZN C 604

Chain	Residue
C	GLU151
C	LYS154
F	HIS57

site_id	AD6
Number of Residues	3
Details	binding site for residue ZN C 605

Chain	Residue
C	HIS209
C	HIS450
C	GTP603

site_id	AD7
Number of Residues	15
Details	binding site for residue GLU D 601

Chain	Residue
D	LYS90
D	GLY91
D	GLY92
D	MET111
D	LYS114
D	LYS126
D	ALA166
D	PRO167
D	ASP168
D	ARG211
D	ASN349
D	GLY377
D	VAL378
D	SER381
D	NDP602

site_id	AD8
Number of Residues	20
Details	binding site for residue NDP D 602

Chain	Residue
D	ALA1
D	ASP168
D	MET169
D	SER170
D	ARG211
D	GLN250
D	PHE252
D	GLY253
D	ASN254
D	VAL255
D	GLU275
D	SER276
D	ALA326
D	SER327
D	GLN330
D	GLY347
D	ALA348
D	ASN349
D	ASN374
D	GLU601

site_id	AD9
Number of Residues	13
Details	binding site for residue GTP D 603

Chain	Residue
D	HIS209
D	GLY210
D	SER213
D	ARG217
D	LEU257
D	HIS258
D	ARG261
D	TYR262
D	ARG265
D	LYS289
D	GLU292
D	HIS450
D	ZN605

site_id	AE1
Number of Residues	2
Details	binding site for residue ZN D 604

Chain	Residue
A	HIS57
D	GLU151

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN D 605

Chain	Residue
D	HIS209
D	ARG217
D	HIS450
D	GTP603

site_id	AE3
Number of Residues	13
Details	binding site for residue GLU E 601

Chain	Residue
E	LYS90
E	GLY92
E	MET111
E	LYS114
E	LYS126
E	ALA166
E	PRO167
E	ASP168
E	ARG211
E	ASN349
E	VAL378
E	SER381
E	NDP602

site_id	AE4
Number of Residues	21
Details	binding site for residue NDP E 602

Chain	Residue
E	PRO167
E	ASP168
E	MET169
E	SER170
E	ARG211
E	THR215
E	GLN250
E	GLY251
E	PHE252
E	GLY253
E	ASN254
E	VAL255
E	GLU275
E	SER276
E	ALA325
E	ALA326
E	GLN330
E	ALA348
E	ASN349
E	ASN374
E	GLU601

site_id	AE5
Number of Residues	13
Details	binding site for residue GTP E 603

Chain	Residue
E	HIS209
E	GLY210
E	SER213
E	ARG217
E	HIS258
E	ARG261
E	TYR262
E	ARG265
E	LYS289
E	GLU292
E	LYS446
E	HIS450
E	ZN605

site_id	AE6
Number of Residues	3
Details	binding site for residue ZN E 604

Chain	Residue
B	HIS57
E	GLU151
E	LYS154

site_id	AE7
Number of Residues	3
Details	binding site for residue ZN E 605

Chain	Residue
E	HIS209
E	HIS450
E	GTP603

site_id	AE8
Number of Residues	3
Details	binding site for residue ZN F 601

Chain	Residue
C	HIS57
F	GLU151
F	LYS154

site_id	AE9
Number of Residues	12
Details	binding site for residue GLU F 602

Chain	Residue
F	LYS90
F	GLY91
F	MET111
F	LYS114
F	LYS126
F	ALA166
F	PRO167
F	ASP168
F	ARG211
F	ASN349
F	SER381
F	NDP603

site_id	AF1
Number of Residues	23
Details	binding site for residue NDP F 603

Chain	Residue
F	ARG94
F	LYS134
F	ASP168
F	MET169
F	SER170
F	ARG211
F	THR215
F	GLN250
F	GLY251
F	PHE252
F	GLY253
F	ASN254
F	VAL255
F	GLU275
F	SER276
F	ALA325
F	ALA326
F	GLN330
F	GLY347
F	ALA348
F	ASN349
F	ASN374
F	GLU602

site_id	AF2
Number of Residues	14
Details	binding site for residue GTP F 604

Chain	Residue
F	HIS209
F	GLY210
F	SER213
F	ARG217
F	LEU257
F	HIS258
F	ARG261
F	TYR262
F	ARG265
F	LYS289
F	GLU292
F	LYS446
F	HIS450
F	ZN605

site_id	AF3
Number of Residues	3
Details	binding site for residue ZN F 605

Chain	Residue
F	HIS209
F	HIS450
F	GTP604

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL120-PRO133

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	54
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	18
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	24
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	48
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)