Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ETE

Crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene

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	20
Details	BINDING SITE FOR RESIDUE NDP A 551

Chain	Residue
A	ARG94
A	ASN254
A	VAL255
A	GLU275
A	SER276
A	ALA326
A	SER327
A	GLN330
A	ALA348
A	ASN349
A	ASN374
A	LYS134
A	GLU550
A	ASP168
A	MET169
A	SER170
A	ARG211
A	THR215
A	PHE252
A	GLY253

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GTP A 553

Chain	Residue
A	ILE212
A	SER213
A	ARG217
A	LEU257
A	HIS258
A	ARG261
A	TYR262
A	GLU292
A	LYS446
A	HIS450

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NDP B 551

Chain	Residue
B	ARG94
B	LYS134
B	PRO167
B	ASP168
B	MET169
B	SER170
B	ARG211
B	THR215
B	GLN250
B	PHE252
B	GLY253
B	ASN254
B	VAL255
B	GLU275
B	SER276
B	ALA326
B	SER327
B	GLN330
B	GLY347
B	ALA348
B	ASN349
B	ASN374
B	GLU550

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GTP B 553

Chain	Residue
B	HIS209
B	ARG217
B	HIS258
B	ARG261
B	TYR262
B	ARG265
B	GLU292
B	HIS450
B	HOH554

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NDP C 551

Chain	Residue
C	ARG94
C	LYS134
C	PRO167
C	ASP168
C	MET169
C	SER170
C	ARG211
C	THR215
C	PHE252
C	GLY253
C	ASN254
C	VAL255
C	GLU275
C	SER276
C	ALA325
C	ALA326
C	GLN330
C	GLY347
C	ASN349
C	ASN374
C	GLU550
C	HOH582
C	HOH590

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GTP C 553

Chain	Residue
C	HIS209
C	ARG217
C	HIS258
C	ARG261
C	TYR262
C	ARG265
C	LYS289
C	GLU292

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NDP D 551

Chain	Residue
D	THR215
D	GLY251
D	PHE252
D	GLY253
D	ASN254
D	VAL255
D	GLU275
D	SER276
D	ALA325
D	ALA326
D	SER327
D	GLN330
D	GLY347
D	ALA348
D	ASN349
D	ASN374
D	GLU550
D	HOH560
D	ARG94
D	LYS134
D	ASP168
D	MET169
D	SER170
D	ARG211

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GTP D 553

Chain	Residue
D	HIS209
D	ARG217
D	HIS258
D	ARG261
D	TYR262
D	ARG265
D	GLU292
D	HIS450
D	HOH554
D	HOH567
D	HOH573
D	HOH586

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NDP E 551

Chain	Residue
E	ARG94
E	LYS134
E	ASP168
E	MET169
E	SER170
E	ARG211
E	THR215
E	GLN250
E	PHE252
E	GLY253
E	ASN254
E	VAL255
E	GLU275
E	SER276
E	ALA325
E	ALA326
E	SER327
E	GLN330
E	ALA348
E	ASN349
E	GLU550

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GTP E 553

Chain	Residue
E	HIS209
E	ARG217
E	LEU257
E	HIS258
E	ARG261
E	TYR262
E	ARG265
E	GLU292
E	HIS450
E	HOH572

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NDP F 551

Chain	Residue
F	ARG94
F	LYS134
F	ASP168
F	MET169
F	ARG211
F	THR215
F	PHE252
F	GLY253
F	ASN254
F	VAL255
F	GLU275
F	SER276
F	ALA326
F	SER327
F	GLN330
F	GLY347
F	ALA348
F	ASN349
F	ASN374

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GTP F 553

Chain	Residue
F	HIS209
F	ARG217
F	HIS258
F	ARG261
F	TYR262
F	ARG265
F	GLU292
F	HIS450

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE H3P B 552

Chain	Residue
A	TYR190
A	H3P552
B	ALA153
B	ILE158
B	TYR183
E	LYS154

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE H3P A 552

Chain	Residue
A	THR186
A	ILE187
A	TYR190
A	HOH560
B	H3P552
E	MET150
E	THR186
E	ILE187
E	HIS189

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE H3P D 552

Chain	Residue
A	ALA153
D	ALA153
D	LYS154
E	TYR190
F	H3P552

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE H3P F 552

Chain	Residue
D	MET150
D	THR186
D	ILE187
D	HIS189
D	H3P552
F	LYS154
F	THR186
F	ILE187
F	TYR190

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE H3P C 552

Chain	Residue
C	ALA153
C	LYS154
C	H3P554
D	TYR190
F	ALA153
F	LYS154
F	HOH572

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE H3P C 554

Chain	Residue
B	THR186
B	ILE187
B	TYR190
C	MET150
C	THR186
C	ILE187
C	HIS189
C	H3P552
C	HOH574

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	ASP168

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

Chain	Residue	Details
B	LYS126
B	ASP168

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

Chain	Residue	Details
C	LYS126
C	ASP168

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

Chain	Residue	Details
D	LYS126
D	ASP168

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

Chain	Residue	Details
E	LYS126
E	ASP168

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

Chain	Residue	Details
F	LYS126
F	ASP168

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