Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VLD

Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and NAD+

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	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	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide binding
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	15
Details	binding site for residue HIS A 501

Chain	Residue
A	LEU174
A	TYR402
A	HIS408
A	NAD502
B	GLU455
B	HIS460
B	ZN501
A	SER176
A	SER277
A	GLN299
A	HIS302
A	GLU367
A	HIS368
A	GLU397
A	ASP401

site_id	AC2
Number of Residues	26
Details	binding site for residue NAD A 502

Chain	Residue
A	PHE96
A	ASP97
A	TYR166
A	PRO168
A	GLY169
A	GLY170
A	THR171
A	PRO198
A	GLY225
A	GLY226
A	GLN228
A	PRO249
A	GLY250
A	ASN251
A	TYR253
A	ALA274
A	GLY275
A	PRO276
A	SER277
A	HIS302
A	GLU367
A	HIS408
A	VAL409
A	LEU410
A	THR412
A	HIS501

site_id	AC3
Number of Residues	5
Details	binding site for residue ZN A 503

Chain	Residue
A	HIS460
B	GLN299
B	HIS302
B	ASP401
B	HIS502

site_id	AC4
Number of Residues	5
Details	binding site for residue PEG A 504

Chain	Residue
A	GLN91
A	TYR92
A	LYS95
E	LYS285
E	GLY316

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

Chain	Residue
A	GLN299
A	HIS302
A	ASP401
A	HIS501
B	HIS460

site_id	AC6
Number of Residues	16
Details	binding site for residue HIS B 502

Chain	Residue
A	GLU455
A	LEU457
A	HIS460
A	ZN503
B	LEU174
B	SER176
B	SER277
B	GLN299
B	HIS302
B	GLU367
B	HIS368
B	GLU397
B	ASP401
B	TYR402
B	HIS408
B	NAD503

site_id	AC7
Number of Residues	28
Details	binding site for residue NAD B 503

Chain	Residue
B	HOH606
B	PHE96
B	ASP97
B	TYR166
B	PRO168
B	GLY169
B	GLY170
B	THR171
B	PRO198
B	GLY225
B	GLY226
B	GLN228
B	PRO249
B	GLY250
B	ASN251
B	TYR253
B	VAL254
B	ALA274
B	GLY275
B	PRO276
B	SER277
B	HIS302
B	GLU367
B	HIS408
B	VAL409
B	LEU410
B	THR412
B	HIS502

site_id	AC8
Number of Residues	5
Details	binding site for residue ZN C 501

Chain	Residue
C	GLN299
C	HIS302
C	ASP401
C	HIS502
D	HIS460

site_id	AC9
Number of Residues	15
Details	binding site for residue HIS 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
C	NAD503
D	GLU455
D	LEU457
D	HIS460

site_id	AD1
Number of Residues	26
Details	binding site for residue NAD C 503

Chain	Residue
C	PHE96
C	ASP97
C	TYR166
C	PRO168
C	GLY169
C	GLY170
C	THR171
C	PRO198
C	GLY225
C	GLN228
C	PRO249
C	GLY250
C	ASN251
C	TYR253
C	VAL254
C	ALA274
C	GLY275
C	PRO276
C	SER277
C	HIS302
C	GLU367
C	HIS408
C	VAL409
C	LEU410
C	THR412
C	HIS502

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN D 501

Chain	Residue
C	HIS460
D	GLN299
D	HIS302
D	ASP401
D	HIS502

site_id	AD3
Number of Residues	16
Details	binding site for residue HIS D 502

Chain	Residue
C	GLU455
C	LEU457
C	HIS460
D	LEU174
D	SER176
D	SER277
D	GLN299
D	HIS302
D	GLU367
D	HIS368
D	GLU397
D	ASP401
D	TYR402
D	HIS408
D	ZN501
D	NAD503

site_id	AD4
Number of Residues	25
Details	binding site for residue NAD D 503

Chain	Residue
D	PHE96
D	ASP97
D	TYR166
D	PRO168
D	GLY169
D	GLY170
D	THR171
D	ALA172
D	PRO198
D	GLN228
D	PRO249
D	GLY250
D	ASN251
D	TYR253
D	ALA274
D	GLY275
D	PRO276
D	SER277
D	HIS302
D	GLU367
D	HIS408
D	VAL409
D	LEU410
D	THR412
D	HIS502

site_id	AD5
Number of Residues	5
Details	binding site for residue ZN E 501

Chain	Residue
E	GLN299
E	HIS302
E	ASP401
E	HIS502
F	HIS460

site_id	AD6
Number of Residues	14
Details	binding site for residue HIS E 502

Chain	Residue
E	SER176
E	SER277
E	GLN299
E	HIS302
E	GLU367
E	HIS368
E	GLU397
E	ASP401
E	TYR402
E	HIS408
E	ZN501
E	NAD503
F	GLU455
F	HIS460

site_id	AD7
Number of Residues	26
Details	binding site for residue NAD E 503

Chain	Residue
E	PHE96
E	ASP97
E	TYR166
E	PRO168
E	GLY169
E	GLY170
E	THR171
E	PRO198
E	GLN228
E	PRO249
E	GLY250
E	ASN251
E	TYR253
E	VAL254
E	ALA274
E	GLY275
E	PRO276
E	SER277
E	HIS302
E	GLU367
E	HIS408
E	VAL409
E	LEU410
E	THR412
E	HIS502
E	HOH607

site_id	AD8
Number of Residues	5
Details	binding site for residue ZN E 504

Chain	Residue
E	HIS460
F	GLN299
F	HIS302
F	ASP401
F	HIS501

site_id	AD9
Number of Residues	15
Details	binding site for residue HIS F 501

Chain	Residue
E	GLU455
E	HIS460
E	ZN504
F	LEU174
F	SER176
F	SER277
F	GLN299
F	HIS302
F	GLU367
F	HIS368
F	GLU397
F	ASP401
F	TYR402
F	HIS408
F	NAD502

site_id	AE1
Number of Residues	28
Details	binding site for residue NAD F 502

Chain	Residue
B	ASN320
F	PHE96
F	ASP97
F	TYR166
F	PRO168
F	GLY169
F	GLY170
F	THR171
F	PRO198
F	GLY225
F	GLY226
F	GLN228
F	PRO249
F	GLY250
F	ASN251
F	TYR253
F	VAL254
F	ALA274
F	GLY275
F	PRO276
F	SER277
F	HIS302
F	GLU367
F	HIS408
F	VAL409
F	LEU410
F	THR412
F	HIS501

site_id	AE2
Number of Residues	2
Details	binding site for residue PEG F 503

Chain	Residue
E	HOH628
F	MET363

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)