Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6G2U

Crystal structure of the human glutamate dehydrogenase 2 (hGDH2)

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	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006536	biological_process	glutamate metabolic process
A	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
A	0070728	molecular_function	L-leucine 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	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0006536	biological_process	glutamate metabolic process
B	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
B	0070728	molecular_function	L-leucine 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	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0006536	biological_process	glutamate metabolic process
C	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
C	0070728	molecular_function	L-leucine 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	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006536	biological_process	glutamate metabolic process
D	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
D	0070728	molecular_function	L-leucine 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	0005515	molecular_function	protein binding
E	0005525	molecular_function	GTP binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0006536	biological_process	glutamate metabolic process
E	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
E	0070728	molecular_function	L-leucine 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	0005515	molecular_function	protein binding
F	0005525	molecular_function	GTP binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0005829	cellular_component	cytosol
F	0006520	biological_process	amino acid metabolic process
F	0006536	biological_process	glutamate metabolic process
F	0006537	biological_process	glutamate biosynthetic 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	0043531	molecular_function	ADP binding
F	0070728	molecular_function	L-leucine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PO4 A 601

Chain	Residue
A	SER397
A	ARG400
A	HOH738
A	HOH785
D	ASP123
D	ARG463

site_id	AC2
Number of Residues	6
Details	binding site for residue PO4 A 602

Chain	Residue
A	LYS450
A	HOH725
A	HOH754
A	ARG221
A	TYR266
A	ARG269

site_id	AC3
Number of Residues	3
Details	binding site for residue PO4 A 603

Chain	Residue
A	ASN394
B	ASN394
D	ASN394

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 A 604

Chain	Residue
A	HIS213
A	GLY214
A	LYS450

site_id	AC5
Number of Residues	1
Details	binding site for residue NA A 605

Chain	Residue
A	GLY478

site_id	AC6
Number of Residues	1
Details	binding site for residue NA A 606

Chain	Residue
A	HOH859

site_id	AC7
Number of Residues	2
Details	binding site for residue CL A 607

Chain	Residue
A	ARG247
C	LYS424

site_id	AC8
Number of Residues	2
Details	binding site for residue CL A 608

Chain	Residue
B	GLY501
B	HOH704

site_id	AC9
Number of Residues	2
Details	binding site for residue CL A 609

Chain	Residue
A	GLU42
A	ARG46

site_id	AD1
Number of Residues	7
Details	binding site for residue PO4 B 601

Chain	Residue
A	ARG463
A	HOH723
B	SER397
B	ARG400
B	HOH702
B	HOH708
B	HOH710

site_id	AD2
Number of Residues	6
Details	binding site for residue PO4 B 602

Chain	Residue
B	ARG265
B	TYR266
B	ARG269
B	HIS454
B	HOH738
B	HOH760

site_id	AD3
Number of Residues	4
Details	binding site for residue PO4 B 603

Chain	Residue
A	THR431
B	ARG423
B	LYS424
E	ARG247

site_id	AD4
Number of Residues	2
Details	binding site for residue PO4 B 604

Chain	Residue
B	TYR194
D	TYR194

site_id	AD5
Number of Residues	2
Details	binding site for residue PO4 B 605

Chain	Residue
B	HIS213
B	GLY214

site_id	AD6
Number of Residues	1
Details	binding site for residue CL B 606

Chain	Residue
B	ASN197

site_id	AD7
Number of Residues	5
Details	binding site for residue PO4 C 601

Chain	Residue
C	ASP123
C	ARG463
C	HOH734
F	SER397
F	ARG400

site_id	AD8
Number of Residues	6
Details	binding site for residue PO4 C 602

Chain	Residue
C	ARG221
C	ARG265
C	TYR266
C	ARG269
C	LYS450
C	HOH711

site_id	AD9
Number of Residues	6
Details	binding site for residue PO4 C 603

Chain	Residue
C	SER397
C	ARG400
C	HOH703
C	HOH720
C	HOH727
E	ARG463

site_id	AE1
Number of Residues	4
Details	binding site for residue PO4 C 604

Chain	Residue
C	NA606
C	HOH719
C	HOH740
E	ALA438

site_id	AE2
Number of Residues	1
Details	binding site for residue PO4 C 605

Chain	Residue
C	LYS293

site_id	AE3
Number of Residues	2
Details	binding site for residue NA C 606

Chain	Residue
C	ARG423
C	PO4604

site_id	AE4
Number of Residues	2
Details	binding site for residue NA C 607

Chain	Residue
C	HOH845
C	HOH857

site_id	AE5
Number of Residues	2
Details	binding site for residue CL C 608

Chain	Residue
C	HIS213
C	HOH909

site_id	AE6
Number of Residues	3
Details	binding site for residue PO4 D 601

Chain	Residue
B	ARG463
D	SER397
D	ARG400

site_id	AE7
Number of Residues	4
Details	binding site for residue PO4 D 602

Chain	Residue
D	ARG221
D	TYR266
D	ARG269
D	HOH758

site_id	AE8
Number of Residues	5
Details	binding site for residue NA D 603

Chain	Residue
D	ILE55
D	ILE56
D	PRO58
D	ASN60
D	HIS86

site_id	AE9
Number of Residues	1
Details	binding site for residue NA D 604

Chain	Residue
D	HOH838

site_id	AF1
Number of Residues	1
Details	binding site for residue NA D 605

Chain	Residue
D	LYS344

site_id	AF2
Number of Residues	1
Details	binding site for residue NA D 606

Chain	Residue
D	CL618

site_id	AF3
Number of Residues	1
Details	binding site for residue NA D 610

Chain	Residue
D	HOH884

site_id	AF4
Number of Residues	4
Details	binding site for residue NA D 611

Chain	Residue
B	HOH853
B	HOH862
D	HOH802
D	HOH982

site_id	AF5
Number of Residues	4
Details	binding site for residue NA D 612

Chain	Residue
D	HOH1001
D	ASP172
D	THR175
D	HOH937

site_id	AF6
Number of Residues	1
Details	binding site for residue CL D 617

Chain	Residue
D	ASP281

site_id	AF7
Number of Residues	1
Details	binding site for residue CL D 618

Chain	Residue
D	NA606

site_id	AF8
Number of Residues	6
Details	binding site for residue PO4 E 601

Chain	Residue
E	HIS213
E	GLY214
E	LYS450
E	HOH721
E	HOH729
E	HOH749

site_id	AF9
Number of Residues	4
Details	binding site for residue PO4 E 602

Chain	Residue
E	ARG221
E	TYR266
E	ARG269
E	LYS450

site_id	AG1
Number of Residues	2
Details	binding site for residue NA E 604

Chain	Residue
E	THR357
E	GLU359

site_id	AG2
Number of Residues	2
Details	binding site for residue CL E 606

Chain	Residue
E	ASP10
E	HOH790

site_id	AG3
Number of Residues	4
Details	binding site for residue CL E 610

Chain	Residue
E	GLY429
E	HOH723
E	HOH887
E	HOH931

site_id	AG4
Number of Residues	1
Details	binding site for residue CL E 611

Chain	Residue
C	LEU393

site_id	AG5
Number of Residues	6
Details	binding site for residue PO4 F 601

Chain	Residue
F	HIS213
F	GLY214
F	LYS450
F	HOH710
F	HOH722
F	HOH761

site_id	AG6
Number of Residues	6
Details	binding site for residue PO4 F 602

Chain	Residue
F	ARG221
F	ARG265
F	TYR266
F	ARG269
F	LYS450
F	HOH759

site_id	AG7
Number of Residues	5
Details	binding site for residue PO4 F 603

Chain	Residue
E	SER397
E	ARG400
F	ASP123
F	ARG463
F	HOH704

site_id	AG8
Number of Residues	4
Details	binding site for residue PO4 F 604

Chain	Residue
C	ASN394
E	ASN394
F	ASN394
F	HOH701

site_id	AG9
Number of Residues	1
Details	binding site for residue PO4 F 605

Chain	Residue
F	TYR194

site_id	AH1
Number of Residues	1
Details	binding site for residue NA F 606

Chain	Residue
C	HOH884

site_id	AH2
Number of Residues	2
Details	binding site for residue NA F 607

Chain	Residue
F	GLU146
F	HOH834

site_id	AH3
Number of Residues	4
Details	binding site for residue NA F 608

Chain	Residue
C	HOH725
F	HIS193
F	ASP195
F	HOH788

site_id	AH4
Number of Residues	1
Details	binding site for residue CL F 609

Chain	Residue
F	ARG23

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	VAL124-PRO137

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	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"16023112","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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