Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VLC

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0000166	molecular_function	nucleotide binding
A	0004399	molecular_function	histidinol dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
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	0000166	molecular_function	nucleotide binding
B	0004399	molecular_function	histidinol dehydrogenase activity
B	0005737	cellular_component	cytoplasm
B	0008652	biological_process	amino acid biosynthetic process
B	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
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	0000166	molecular_function	nucleotide binding
C	0004399	molecular_function	histidinol dehydrogenase activity
C	0005737	cellular_component	cytoplasm
C	0008652	biological_process	amino acid biosynthetic process
C	0009507	cellular_component	chloroplast
C	0009536	cellular_component	plastid
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	0000166	molecular_function	nucleotide binding
D	0004399	molecular_function	histidinol dehydrogenase activity
D	0005737	cellular_component	cytoplasm
D	0008652	biological_process	amino acid biosynthetic process
D	0009507	cellular_component	chloroplast
D	0009536	cellular_component	plastid
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	0000166	molecular_function	nucleotide binding
E	0004399	molecular_function	histidinol dehydrogenase activity
E	0005737	cellular_component	cytoplasm
E	0008652	biological_process	amino acid biosynthetic process
E	0009507	cellular_component	chloroplast
E	0009536	cellular_component	plastid
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	0000166	molecular_function	nucleotide binding
F	0004399	molecular_function	histidinol dehydrogenase activity
F	0005737	cellular_component	cytoplasm
F	0008652	biological_process	amino acid biosynthetic process
F	0009507	cellular_component	chloroplast
F	0009536	cellular_component	plastid
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	13
Details	binding site for residue HSO A 501

Chain	Residue
A	SER176
B	GLU455
B	LEU457
B	HIS460
B	ZN501
A	GLN299
A	HIS302
A	GLU367
A	HIS368
A	GLU397
A	ASP401
A	TYR402
A	HIS408

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 502

Chain	Residue
A	HIS460
B	GLN299
B	HIS302
B	ASP401
B	HSO502

site_id	AC3
Number of Residues	5
Details	binding site for residue ZN B 501

Chain	Residue
A	GLN299
A	HIS302
A	ASP401
A	HSO501
B	HIS460

site_id	AC4
Number of Residues	15
Details	binding site for residue HSO B 502

Chain	Residue
A	GLU455
A	LEU457
A	HIS460
A	ZN502
B	LEU174
B	SER176
B	SER277
B	GLN299
B	HIS302
B	GLU367
B	HIS368
B	GLU397
B	ASP401
B	TYR402
B	HIS408

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN C 501

Chain	Residue
C	GLN299
C	HIS302
C	ASP401
C	HSO502
D	HIS460

site_id	AC6
Number of Residues	14
Details	binding site for residue HSO C 502

Chain	Residue
C	SER176
C	SER277
C	GLN299
C	HIS302
C	GLU367
C	HIS368
C	GLU397
C	ASP401
C	TYR402
C	HIS408
C	ZN501
D	GLU455
D	LEU457
D	HIS460

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

Chain	Residue
C	HIS460
D	GLN299
D	HIS302
D	ASP401
D	HSO502

site_id	AC8
Number of Residues	14
Details	binding site for residue HSO D 502

Chain	Residue
C	GLU455
C	LEU457
C	HIS460
D	SER176
D	SER277
D	GLN299
D	HIS302
D	GLU367
D	HIS368
D	GLU397
D	ASP401
D	TYR402
D	HIS408
D	ZN501

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN E 501

Chain	Residue
E	GLN299
E	HIS302
E	ASP401
E	HSO502
F	HIS460

site_id	AD1
Number of Residues	13
Details	binding site for residue HSO E 502

Chain	Residue
E	SER176
E	GLN299
E	HIS302
E	GLU367
E	HIS368
E	GLU397
E	ASP401
E	TYR402
E	HIS408
E	ZN501
F	GLU455
F	LEU457
F	HIS460

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN E 503

Chain	Residue
E	HIS460
F	GLN299
F	HIS302
F	ASP401
F	HSO501

site_id	AD3
Number of Residues	15
Details	binding site for residue HSO F 501

Chain	Residue
E	GLU455
E	LEU457
E	HIS460
E	ZN503
F	LEU174
F	SER176
F	SER277
F	GLN299
F	HIS302
F	GLU367
F	HIS368
F	GLU397
F	ASP401
F	TYR402
F	HIS408

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)