Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6YEI

Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD

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	0005507	molecular_function	copper ion binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0006520	biological_process	amino acid metabolic process
A	0006538	biological_process	L-glutamate catabolic process
A	0008270	molecular_function	zinc ion binding
A	0009536	cellular_component	plastid
A	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
A	0050897	molecular_function	cobalt ion 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	0005507	molecular_function	copper ion binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0006520	biological_process	amino acid metabolic process
B	0006538	biological_process	L-glutamate catabolic process
B	0008270	molecular_function	zinc ion binding
B	0009536	cellular_component	plastid
B	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
B	0050897	molecular_function	cobalt ion 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	0005507	molecular_function	copper ion binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0006520	biological_process	amino acid metabolic process
C	0006538	biological_process	L-glutamate catabolic process
C	0008270	molecular_function	zinc ion binding
C	0009536	cellular_component	plastid
C	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
C	0050897	molecular_function	cobalt ion 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	0005507	molecular_function	copper ion binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0006520	biological_process	amino acid metabolic process
D	0006538	biological_process	L-glutamate catabolic process
D	0008270	molecular_function	zinc ion binding
D	0009536	cellular_component	plastid
D	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
D	0050897	molecular_function	cobalt ion 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	0005507	molecular_function	copper ion binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0006520	biological_process	amino acid metabolic process
E	0006538	biological_process	L-glutamate catabolic process
E	0008270	molecular_function	zinc ion binding
E	0009536	cellular_component	plastid
E	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
E	0050897	molecular_function	cobalt ion 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	0005507	molecular_function	copper ion binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0006520	biological_process	amino acid metabolic process
F	0006538	biological_process	L-glutamate catabolic process
F	0008270	molecular_function	zinc ion binding
F	0009536	cellular_component	plastid
F	0009646	biological_process	response to absence of light
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	0019740	biological_process	nitrogen utilization
F	0050897	molecular_function	cobalt ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue NAD A 501

Chain	Residue
A	THR185
A	LEU290
A	ALA310
A	ALA311
A	ASN312
A	ASN337
A	HOH629
A	HOH651
A	HOH709
A	PHE214
A	GLY215
A	ASN216
A	VAL217
A	ASP237
A	ILE238
A	ALA288
A	ALA289

site_id	AC2
Number of Residues	6
Details	binding site for residue MPD A 502

Chain	Residue
A	TYR163
A	GLY176
A	ASN351
A	GLY354
A	PHE355
E	PRO97

site_id	AC3
Number of Residues	4
Details	binding site for residue MPD A 503

Chain	Residue
A	LYS36
A	PHE54
A	VAL75
A	PRO77

site_id	AC4
Number of Residues	4
Details	binding site for residue MPD A 504

Chain	Residue
A	GLU199
A	HIS200
A	CYS386
A	HOH695

site_id	AC5
Number of Residues	4
Details	binding site for residue MPD A 505

Chain	Residue
A	SER219
A	TRP220
A	LYS223
A	LYS258

site_id	AC6
Number of Residues	6
Details	binding site for residue K A 506

Chain	Residue
A	SER27
A	ILE30
A	HOH608
A	HOH702
B	GLU38
B	HOH721

site_id	AC7
Number of Residues	6
Details	binding site for residue K A 507

Chain	Residue
A	GLU38
B	SER27
B	ILE30
B	HOH644
B	HOH682
B	HOH712

site_id	AC8
Number of Residues	6
Details	binding site for residue MRD A 508

Chain	Residue
A	TYR71
A	ILE114
A	LEU117
A	GLY144
A	THR149
A	HOH602

site_id	AC9
Number of Residues	13
Details	binding site for residue NAD B 501

Chain	Residue
B	THR185
B	PHE214
B	GLY215
B	ASN216
B	VAL217
B	ASP237
B	ILE238
B	ALA288
B	ALA289
B	LEU290
B	ASN312
B	ASN337
B	HOH621

site_id	AD1
Number of Residues	6
Details	binding site for residue MPD B 502

Chain	Residue
B	TYR163
B	LEU175
B	GLY176
B	ASN351
B	GLY354
D	PRO97

site_id	AD2
Number of Residues	5
Details	binding site for residue MPD B 503

Chain	Residue
B	GLU34
B	LYS36
B	PHE54
B	VAL56
B	PRO77

site_id	AD3
Number of Residues	3
Details	binding site for residue MPD B 504

Chain	Residue
B	LEU196
B	HIS200
B	LEU388

site_id	AD4
Number of Residues	6
Details	binding site for residue MRD B 505

Chain	Residue
B	TYR71
B	ILE114
B	GLY144
B	GLN148
B	THR149
B	TRP152

site_id	AD5
Number of Residues	14
Details	binding site for residue NAD C 501

Chain	Residue
C	ASN337
C	THR185
C	GLY213
C	PHE214
C	GLY215
C	ASN216
C	VAL217
C	ASP237
C	ILE238
C	ALA288
C	ALA289
C	LEU290
C	ALA311
C	ASN312

site_id	AD6
Number of Residues	6
Details	binding site for residue MPD C 502

Chain	Residue
A	PRO97
C	TYR163
C	GLY176
C	ASN351
C	GLY354
C	PHE355

site_id	AD7
Number of Residues	5
Details	binding site for residue MPD C 503

Chain	Residue
C	GLU34
C	LYS36
C	PHE54
C	VAL75
C	PRO77

site_id	AD8
Number of Residues	6
Details	binding site for residue MRD C 504

Chain	Residue
C	LEU117
C	GLY144
C	GLN148
C	THR149
C	TRP152
C	HOH643

site_id	AD9
Number of Residues	6
Details	binding site for residue K C 505

Chain	Residue
C	SER27
C	ILE30
C	HOH663
C	HOH676
C	HOH689
D	GLU38

site_id	AE1
Number of Residues	1
Details	binding site for residue EDO D 501

Chain	Residue
D	ASP44

site_id	AE2
Number of Residues	15
Details	binding site for residue NAD D 502

Chain	Residue
D	THR185
D	PHE214
D	GLY215
D	ASN216
D	VAL217
D	ASP237
D	ILE238
D	ALA288
D	ALA289
D	LEU290
D	ALA311
D	ASN312
D	ASN337
D	HOH612
D	HOH637

site_id	AE3
Number of Residues	5
Details	binding site for residue MPD D 503

Chain	Residue
D	GLU34
D	LYS36
D	PHE54
D	VAL56
D	PRO77

site_id	AE4
Number of Residues	8
Details	binding site for residue MPD D 504

Chain	Residue
D	TYR163
D	ASP174
D	GLY176
D	ASN351
D	GLY354
D	PHE355
F	PRO97
F	HOH620

site_id	AE5
Number of Residues	4
Details	binding site for residue MPD D 505

Chain	Residue
D	SER219
D	TRP220
D	LYS223
D	LEU254

site_id	AE6
Number of Residues	4
Details	binding site for residue MPD D 506

Chain	Residue
D	LEU196
D	HIS200
D	VAL329
D	LEU388

site_id	AE7
Number of Residues	6
Details	binding site for residue K D 507

Chain	Residue
C	GLU38
D	SER27
D	ILE30
D	HOH602
D	HOH677
D	HOH704

site_id	AE8
Number of Residues	5
Details	binding site for residue MRD D 508

Chain	Residue
D	TYR71
D	ILE114
D	GLY144
D	THR149
D	TRP152

site_id	AE9
Number of Residues	5
Details	binding site for residue MPD E 501

Chain	Residue
D	ASP44
D	SER115
D	HOH690
E	ASP44
E	ARG119

site_id	AF1
Number of Residues	14
Details	binding site for residue NAD E 502

Chain	Residue
E	THR185
E	GLY213
E	PHE214
E	GLY215
E	ASN216
E	VAL217
E	ASP237
E	ILE238
E	ALA289
E	LEU290
E	ALA310
E	ALA311
E	ASN312
E	ASN337

site_id	AF2
Number of Residues	4
Details	binding site for residue MPD E 503

Chain	Residue
E	GLU34
E	PHE54
E	VAL56
E	VAL75

site_id	AF3
Number of Residues	6
Details	binding site for residue K E 504

Chain	Residue
E	SER27
E	ILE30
E	HOH619
E	HOH647
F	GLU38
F	HOH732

site_id	AF4
Number of Residues	7
Details	binding site for residue MRD E 505

Chain	Residue
E	TYR71
E	ILE114
E	GLY144
E	GLN148
E	THR149
E	TRP152
E	HOH620

site_id	AF5
Number of Residues	6
Details	binding site for residue K E 506

Chain	Residue
E	GLU38
F	SER27
F	ILE30
F	HOH628
F	HOH688
F	HOH725

site_id	AF6
Number of Residues	28
Details	binding site for residue NAD F 501

Chain	Residue
F	ARG70
F	ASP142
F	MET143
F	GLY144
F	ARG181
F	THR185
F	PHE214
F	GLY215
F	ASN216
F	VAL217
F	ASP237
F	ILE238
F	ALA288
F	ALA289
F	LEU290
F	ALA310
F	ALA311
F	ASN312
F	ASN337
F	AKG502
F	HOH645
F	HOH650
F	HOH652
F	HOH656
F	HOH663
F	HOH681
F	HOH686
F	HOH700

site_id	AF7
Number of Residues	14
Details	binding site for residue AKG F 502

Chain	Residue
F	LYS66
F	GLY68
F	MET87
F	LYS90
F	LYS102
F	ALA140
F	ASP142
F	ARG181
F	ASN312
F	GLY340
F	VAL341
F	SER344
F	NAD501
F	HOH626

site_id	AF8
Number of Residues	2
Details	binding site for residue EDO F 503

Chain	Residue
F	GLU34
F	PRO77

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE96-PRO109

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

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