Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HWY

BOVINE GLUTAMATE DEHYDROGENASE COMPLEXED WITH NAD AND 2-OXOGLUTARATE

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	7
Details	BINDING SITE FOR RESIDUE PO4 E 502

Chain	Residue
E	SER213
E	ARG261
E	TYR262
E	PO4503
E	PO4505
E	HOH511
E	HOH512

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 502

Chain	Residue
D	TYR262
D	PO4503
D	PO4505
D	HOH509
D	HOH510
D	SER213
D	ARG261

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 502

Chain	Residue
C	SER213
C	ARG261
C	TYR262
C	PO4503
C	PO4504
C	HOH509
C	HOH510

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 502

Chain	Residue
B	SER213
B	ARG261
B	TYR262
B	PO4503
B	PO4504
B	HOH511
B	HOH512

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 502

Chain	Residue
F	ARG217
F	HIS450
F	HOH510
F	HOH513

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 F 503

Chain	Residue
F	SER213
F	ARG261
F	TYR262
F	PO4504
F	PO4505
F	HOH511
F	HOH512

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 504

Chain	Residue
F	HIS209
F	GLY210
F	PO4503
F	PO4505

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 503

Chain	Residue
E	HIS209
E	GLY210
E	PO4502
E	PO4505

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 503

Chain	Residue
D	HIS209
D	GLY210
D	PO4502
D	PO4505

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 503

Chain	Residue
C	HIS209
C	GLY210
C	PO4502
C	PO4504

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 503

Chain	Residue
B	HIS209
B	GLY210
B	PO4502
B	PO4504

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 504

Chain	Residue
E	ARG217
E	HIS450
E	HOH510
E	HOH513

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 504

Chain	Residue
B	PO4502
B	PO4503
B	HOH510
B	HOH512

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
A	HIS209
A	GLY210
A	PO4503
A	PO4505

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 503

Chain	Residue
A	SER213
A	ARG261
A	TYR262
A	PO4502
A	PO4505
A	HOH509
A	HOH510

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 504

Chain	Residue
A	ARG217
A	HIS450
A	HOH511
A	HOH514

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 505

Chain	Residue
A	PO4502
A	PO4503
A	HOH510
A	HOH514

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 504

Chain	Residue
C	PO4502
C	PO4503
C	HOH510
C	HOH514

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 504

Chain	Residue
D	ARG217
D	HIS450
D	HOH511
D	HOH514

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 505

Chain	Residue
C	ARG217
C	HIS450
C	HOH511
C	HOH514

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 505

Chain	Residue
B	HIS450
B	HOH510
B	HOH513
B	ARG217

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 505

Chain	Residue
F	PO4503
F	PO4504
F	HOH510
F	HOH512

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 505

Chain	Residue
E	PO4502
E	PO4503
E	HOH510
E	HOH512

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 505

Chain	Residue
D	PO4502
D	PO4503
D	HOH510
D	HOH514

site_id	CC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG F 506

Chain	Residue
F	LYS90
F	GLY92
F	MET111
F	LYS114
F	LYS126
F	ALA166
F	PRO167
F	ASN168
F	THR199
F	ARG211
F	ASN349
F	ASN374
F	VAL378
F	SER381
F	NAD507

site_id	CC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG D 506

Chain	Residue
D	LYS90
D	GLY92
D	MET111
D	LYS114
D	LYS126
D	ALA166
D	PRO167
D	ASN168
D	THR199
D	ARG211
D	ASN349
D	ASN374
D	VAL378
D	SER381
D	NAD508

site_id	CC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG C 506

Chain	Residue
C	LYS90
C	GLY92
C	MET111
C	LYS114
C	LYS126
C	ALA166
C	PRO167
C	ASN168
C	THR199
C	ARG211
C	ASN349
C	ASN374
C	VAL378
C	SER381
C	NAD508

site_id	DC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG E 506

Chain	Residue
E	LYS90
E	GLY92
E	MET111
E	LYS114
E	LYS126
E	ALA166
E	PRO167
E	ASN168
E	THR199
E	ARG211
E	ASN349
E	ASN374
E	VAL378
E	SER381
E	NAD508

site_id	DC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG B 506

Chain	Residue
B	LYS90
B	GLY92
B	MET111
B	LYS114
B	LYS126
B	ALA166
B	PRO167
B	ASN168
B	THR199
B	ARG211
B	ASN349
B	ASN374
B	VAL378
B	SER381
B	NAD508

site_id	DC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG A 506

Chain	Residue
A	LYS90
A	GLY92
A	MET111
A	LYS114
A	LYS126
A	ALA166
A	PRO167
A	ASN168
A	THR199
A	ARG211
A	ASN349
A	ASN374
A	VAL378
A	SER381
A	NAD508

site_id	DC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD D 507

Chain	Residue
C	GLN85
C	ARG86
C	THR87
C	CYS115
C	ALA116
C	ASP119
C	VAL120
C	PRO121
C	ARG459
C	LYS488
C	VAL489
D	HIS195
D	GLN205
D	GLY206
D	LYS387
D	ASN388
D	ASN390
D	HIS391
D	VAL392
D	SER393
D	ARG396
D	GLU445

site_id	DC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD A 507

Chain	Residue
A	HIS195
A	GLN205
A	GLY206
A	LYS387
A	ASN388
A	ASN390
A	HIS391
A	VAL392
A	SER393
A	ARG396
B	GLN85
B	ARG86
B	THR87
B	CYS115
B	ALA116
B	ASP119
B	VAL120
B	PRO121
B	ARG459
B	LYS488
B	VAL489

site_id	DC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD F 507

Chain	Residue
F	ARG94
F	ASN168
F	MET169
F	SER170
F	ARG211
F	THR215
F	GLY251
F	PHE252
F	GLY253
F	ASN254
F	VAL255
F	GLU275
F	SER276
F	LYS295
F	ALA325
F	ALA326
F	SER327
F	GLN330
F	GLY347
F	ALA348
F	ASN349
F	ASN374
F	AKG506

site_id	DC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD E 507

Chain	Residue
D	GLN85
D	ARG86
D	THR87
D	CYS115
D	ALA116
D	ASP119
D	VAL120
D	PRO121
D	ARG459
D	LYS488
D	VAL489
E	HIS195
E	GLY206
E	LYS387
E	ASN388
E	ASN390
E	HIS391
E	VAL392
E	SER393
E	ARG396
E	GLU445

site_id	DC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD B 507

Chain	Residue
B	HIS195
B	GLN205
B	GLY206
B	LYS387
B	ASN388
B	ASN390
B	HIS391
B	VAL392
B	SER393
B	ARG396
B	GLU445
F	GLN85
F	ARG86
F	THR87
F	CYS115
F	ALA116
F	ASP119
F	VAL120
F	PRO121
F	ARG459
F	LYS488
F	VAL489

site_id	DC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD C 507

Chain	Residue
C	HIS195
C	GLN205
C	GLY206
C	LYS387
C	ASN388
C	ASN390
C	HIS391
C	VAL392
C	SER393
C	ARG396
C	GLU445
E	GLN85
E	ARG86
E	THR87
E	CYS115
E	ALA116
E	ASP119
E	VAL120
E	PRO121
E	ARG459
E	LYS488
E	VAL489

site_id	EC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD C 508

Chain	Residue
C	ARG94
C	ASN168
C	MET169
C	SER170
C	ARG211
C	THR215
C	GLY251
C	PHE252
C	GLY253
C	ASN254
C	VAL255
C	GLU275
C	SER276
C	LYS295
C	ALA325
C	ALA326
C	SER327
C	GLN330
C	GLY347
C	ALA348
C	ASN349
C	ASN374
C	AKG506

site_id	EC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD A 508

Chain	Residue
A	ARG94
A	ASN168
A	MET169
A	SER170
A	ARG211
A	THR215
A	GLY251
A	PHE252
A	GLY253
A	ASN254
A	VAL255
A	GLU275
A	SER276
A	LYS295
A	ALA325
A	ALA326
A	SER327
A	GLN330
A	GLY347
A	ALA348
A	ASN349
A	ASN374
A	AKG506

site_id	EC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD F 508

Chain	Residue
A	GLN85
A	ARG86
A	THR87
A	CYS115
A	ALA116
A	ASP119
A	VAL120
A	PRO121
A	ARG459
A	LYS488
A	VAL489
F	HIS195
F	GLN205
F	GLY206
F	LYS387
F	ASN388
F	ASN390
F	HIS391
F	VAL392
F	SER393
F	ARG396
F	GLU445

site_id	EC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD B 508

Chain	Residue
B	ARG94
B	ASN168
B	MET169
B	SER170
B	ARG211
B	THR215
B	GLY251
B	PHE252
B	GLY253
B	ASN254
B	VAL255
B	GLU275
B	SER276
B	LYS295
B	ALA325
B	ALA326
B	SER327
B	GLN330
B	GLY347
B	ALA348
B	ASN349
B	ASN374
B	AKG506

site_id	EC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD D 508

Chain	Residue
D	ARG94
D	ASN168
D	MET169
D	SER170
D	ARG211
D	THR215
D	GLY251
D	PHE252
D	GLY253
D	ASN254
D	VAL255
D	GLU275
D	SER276
D	LYS295
D	ALA325
D	ALA326
D	SER327
D	GLN330
D	GLY347
D	ALA348
D	ASN349
D	ASN374
D	AKG506

site_id	EC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD E 508

Chain	Residue
E	ARG94
E	ASN168
E	MET169
E	SER170
E	ARG211
E	THR215
E	GLY251
E	PHE252
E	GLY253
E	ASN254
E	VAL255
E	GLU275
E	SER276
E	LYS295
E	ALA325
E	ALA326
E	SER327
E	GLN330
E	GLY347
E	ALA348
E	ASN349
E	ASN374
E	AKG506

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_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	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_FI4
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_FI5
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
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_FI7
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_FI8
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
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_FI11
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_FI12
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_FI13
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

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	LYS126
A	ASN168

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

Chain	Residue	Details
B	LYS126
B	ASN168

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

Chain	Residue	Details
C	LYS126
C	ASN168

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

Chain	Residue	Details
D	LYS126
D	ASN168

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

Chain	Residue	Details
E	LYS126
E	ASN168

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

Chain	Residue	Details
F	LYS126
F	ASN168

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