Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4XGI

Crystal structure of Glutamate dehydrogenase from Burkholderia thailandensis

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	0006520	biological_process	amino acid metabolic 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
B	0000166	molecular_function	nucleotide binding
B	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
B	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
B	0006520	biological_process	amino acid metabolic 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
C	0000166	molecular_function	nucleotide binding
C	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
C	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
C	0006520	biological_process	amino acid metabolic 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
D	0000166	molecular_function	nucleotide binding
D	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
D	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
D	0006520	biological_process	amino acid metabolic 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
E	0000166	molecular_function	nucleotide binding
E	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
E	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
E	0006520	biological_process	amino acid metabolic 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
F	0000166	molecular_function	nucleotide binding
F	0004352	molecular_function	glutamate dehydrogenase (NAD+) activity
F	0004353	molecular_function	glutamate dehydrogenase [NAD(P)+] activity
F	0006520	biological_process	amino acid metabolic 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue NAD A 500

Chain	Residue
A	ARG92
A	GLY238
A	ASN239
A	VAL240
A	ASP260
A	HIS261
A	ALA311
A	ALA312
A	GLY333
A	ALA334
A	ASN335
A	ASP164
A	ASN360
A	AKG501
A	HOH639
A	HOH661
A	HOH688
A	HOH691
A	HOH703
A	HOH756
A	HOH779
A	HOH849
A	VAL165
A	ASN166
A	ARG204
A	THR208
A	GLN235
A	GLY236
A	PHE237

site_id	AC2
Number of Residues	11
Details	binding site for residue AKG A 501

Chain	Residue
A	LYS88
A	GLY90
A	MET109
A	LYS112
A	LYS124
A	ALA162
A	ARG204
A	ASN335
A	SER367
A	NAD500
A	HOH843

site_id	AC3
Number of Residues	1
Details	binding site for residue EDO A 502

Chain	Residue
A	VAL409

site_id	AC4
Number of Residues	32
Details	binding site for residue NAD B 500

Chain	Residue
B	ARG92
B	ASP164
B	VAL165
B	ASN166
B	ARG204
B	THR208
B	GLN235
B	GLY236
B	PHE237
B	GLY238
B	ASN239
B	VAL240
B	ASP260
B	HIS261
B	ALA311
B	ALA312
B	LEU313
B	GLY333
B	ALA334
B	ASN335
B	ASN360
B	AKG501
B	HOH640
B	HOH648
B	HOH671
B	HOH682
B	HOH721
B	HOH723
B	HOH768
B	HOH774
B	HOH864
B	HOH881

site_id	AC5
Number of Residues	13
Details	binding site for residue AKG B 501

Chain	Residue
B	LYS88
B	GLY90
B	MET109
B	LYS112
B	LYS124
B	ALA162
B	ARG204
B	ASN335
B	GLY363
B	VAL364
B	SER367
B	NAD500
B	HOH655

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO B 502

Chain	Residue
B	TRP401
B	ALA404
B	VAL409
B	HOH882

site_id	AC7
Number of Residues	31
Details	binding site for residue NAD C 500

Chain	Residue
C	GLY238
C	ASN239
C	VAL240
C	ASP260
C	HIS261
C	ALA311
C	ALA312
C	GLY333
C	ALA334
C	ASN335
C	ASN360
C	AKG501
C	HOH609
C	HOH629
C	HOH658
C	HOH661
C	HOH675
C	HOH683
C	HOH759
C	HOH763
C	HOH774
C	HOH783
C	ARG92
C	ASP164
C	VAL165
C	ASN166
C	ARG204
C	THR208
C	GLN235
C	GLY236
C	PHE237

site_id	AC8
Number of Residues	13
Details	binding site for residue AKG C 501

Chain	Residue
C	LYS88
C	GLY89
C	GLY90
C	MET109
C	LYS112
C	LYS124
C	ALA162
C	ARG204
C	ASN335
C	VAL364
C	SER367
C	NAD500
C	HOH796

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO C 502

Chain	Residue
C	ALA404
C	GLU405
C	VAL409

site_id	AD1
Number of Residues	30
Details	binding site for residue NAD D 500

Chain	Residue
D	ARG92
D	ASP164
D	VAL165
D	ASN166
D	ARG204
D	THR208
D	GLY236
D	PHE237
D	GLY238
D	ASN239
D	VAL240
D	ASP260
D	HIS261
D	ALA311
D	ALA312
D	GLY333
D	ALA334
D	ASN335
D	ASN360
D	AKG501
D	HOH651
D	HOH659
D	HOH665
D	HOH679
D	HOH695
D	HOH750
D	HOH777
D	HOH811
D	HOH889
D	HOH900

site_id	AD2
Number of Residues	16
Details	binding site for residue AKG D 501

Chain	Residue
D	LYS88
D	GLY89
D	GLY90
D	MET109
D	LYS112
D	LYS124
D	ALA162
D	PRO163
D	ASP164
D	ARG204
D	ASN335
D	GLY363
D	VAL364
D	SER367
D	NAD500
D	HOH890

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO D 502

Chain	Residue
D	ALA404
D	GLU405
D	VAL409
D	HOH867

site_id	AD4
Number of Residues	31
Details	binding site for residue NAD E 500

Chain	Residue
E	ARG92
E	ASP164
E	VAL165
E	ASN166
E	ARG204
E	THR208
E	GLN235
E	GLY236
E	PHE237
E	GLY238
E	ASN239
E	VAL240
E	ASP260
E	HIS261
E	ALA311
E	ALA312
E	GLY333
E	ALA334
E	ASN335
E	ASN360
E	AKG501
E	HOH607
E	HOH633
E	HOH634
E	HOH645
E	HOH651
E	HOH658
E	HOH724
E	HOH754
E	HOH759
E	HOH826

site_id	AD5
Number of Residues	14
Details	binding site for residue AKG E 501

Chain	Residue
E	LYS88
E	GLY90
E	MET109
E	LYS112
E	LYS124
E	ALA162
E	PRO163
E	ASP164
E	ARG204
E	ASN335
E	VAL364
E	SER367
E	NAD500
E	HOH682

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO E 502

Chain	Residue
E	VAL409
E	HOH823

site_id	AD7
Number of Residues	28
Details	binding site for residue NAD F 500

Chain	Residue
F	ARG92
F	ASP164
F	VAL165
F	ASN166
F	ARG204
F	THR208
F	GLN235
F	GLY236
F	PHE237
F	GLY238
F	ASN239
F	VAL240
F	ASP260
F	HIS261
F	ALA311
F	ALA312
F	LEU313
F	GLY333
F	ALA334
F	ASN335
F	AKG501
F	HOH626
F	HOH645
F	HOH649
F	HOH668
F	HOH736
F	HOH800
F	HOH802

site_id	AD8
Number of Residues	14
Details	binding site for residue AKG F 501

Chain	Residue
F	LYS88
F	GLY89
F	GLY90
F	MET109
F	LYS112
F	LYS124
F	ALA162
F	ARG204
F	ASN335
F	GLY363
F	VAL364
F	SER367
F	NAD500
F	HOH727

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO F 502

Chain	Residue
F	ALA404
F	VAL409

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL118-PRO131

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