Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VLB

Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with Imidazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0004399	molecular_function	histidinol dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0009507	cellular_component	chloroplast
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
B	0000105	biological_process	L-histidine biosynthetic process
B	0004399	molecular_function	histidinol dehydrogenase activity
B	0005737	cellular_component	cytoplasm
B	0009507	cellular_component	chloroplast
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
C	0000105	biological_process	L-histidine biosynthetic process
C	0004399	molecular_function	histidinol dehydrogenase activity
C	0005737	cellular_component	cytoplasm
C	0009507	cellular_component	chloroplast
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
D	0000105	biological_process	L-histidine biosynthetic process
D	0004399	molecular_function	histidinol dehydrogenase activity
D	0005737	cellular_component	cytoplasm
D	0009507	cellular_component	chloroplast
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0046872	molecular_function	metal ion binding
D	0051287	molecular_function	NAD binding
E	0000105	biological_process	L-histidine biosynthetic process
E	0004399	molecular_function	histidinol dehydrogenase activity
E	0005737	cellular_component	cytoplasm
E	0009507	cellular_component	chloroplast
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0046872	molecular_function	metal ion binding
E	0051287	molecular_function	NAD binding
F	0000105	biological_process	L-histidine biosynthetic process
F	0004399	molecular_function	histidinol dehydrogenase activity
F	0005737	cellular_component	cytoplasm
F	0009507	cellular_component	chloroplast
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0046872	molecular_function	metal ion binding
F	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue ZN A 501

Chain	Residue
A	HIS302
A	ASP401
A	IMD502
A	HOH618
A	HOH636
B	HIS460

site_id	AC2
Number of Residues	9
Details	binding site for residue IMD A 502

Chain	Residue
A	TYR402
A	HIS408
A	ZN501
A	HOH618
B	GLU455
B	HIS460
A	SER176
A	HIS302
A	ASP401

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

Chain	Residue
A	THR237
A	GLU238
A	CYS240
A	LYS242

site_id	AC4
Number of Residues	6
Details	binding site for residue ZN A 504

Chain	Residue
A	HIS460
A	IMD505
B	HIS302
B	ASP401
B	HOH642
B	HOH656

site_id	AC5
Number of Residues	10
Details	binding site for residue IMD A 505

Chain	Residue
A	GLU455
A	LEU457
A	HIS460
A	ZN504
B	SER176
B	HIS302
B	ASP401
B	TYR402
B	HIS408
B	HOH656

site_id	AC6
Number of Residues	2
Details	binding site for residue PEG B 501

Chain	Residue
B	THR237
B	GLU238

site_id	AC7
Number of Residues	5
Details	binding site for residue ZN C 501

Chain	Residue
C	HIS302
C	ASP401
C	IMD502
D	HIS460
D	HOH621

site_id	AC8
Number of Residues	8
Details	binding site for residue IMD C 502

Chain	Residue
C	HIS302
C	ASP401
C	TYR402
C	HIS408
C	ZN501
D	GLU455
D	LEU457
D	HIS460

site_id	AC9
Number of Residues	3
Details	binding site for residue PEG C 503

Chain	Residue
C	THR237
C	CYS240
C	LYS242

site_id	AD1
Number of Residues	5
Details	binding site for residue ZN C 504

Chain	Residue
C	HIS460
C	IMD505
C	HOH640
D	HIS302
D	ASP401

site_id	AD2
Number of Residues	6
Details	binding site for residue IMD C 505

Chain	Residue
C	GLU455
C	HIS460
C	ZN504
D	HIS302
D	ASP401
D	TYR402

site_id	AD3
Number of Residues	4
Details	binding site for residue PEG D 501

Chain	Residue
D	THR237
D	GLU238
D	THR239
D	LYS242

site_id	AD4
Number of Residues	6
Details	binding site for residue ZN E 501

Chain	Residue
E	HIS302
E	ASP401
E	IMD502
E	HOH615
E	HOH625
F	HIS460

site_id	AD5
Number of Residues	9
Details	binding site for residue IMD E 502

Chain	Residue
E	SER176
E	HIS302
E	ASP401
E	TYR402
E	HIS408
E	ZN501
F	GLU455
F	LEU457
F	HIS460

site_id	AD6
Number of Residues	5
Details	binding site for residue PEG E 503

Chain	Residue
E	THR237
E	GLU238
E	THR239
E	CYS240
E	LYS242

site_id	AD7
Number of Residues	6
Details	binding site for residue ZN E 504

Chain	Residue
E	HIS460
E	IMD505
F	HIS302
F	ASP401
F	HOH631
F	HOH639

site_id	AD8
Number of Residues	9
Details	binding site for residue IMD E 505

Chain	Residue
F	ASP401
F	TYR402
F	HIS408
F	HOH631
E	GLU455
E	LEU457
E	HIS460
E	ZN504
F	HIS302

site_id	AD9
Number of Residues	2
Details	binding site for residue PEG F 501

Chain	Residue
F	PRO241
F	LYS242

Functional Information from PROSITE/UniProt

site_id	PS00611
Number of Residues	33
Details	HISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmp.AGPSEVLVIAdkhAipsh..VAADLLSqaEH

Chain	Residue	Details
A	ILE270-HIS302

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