4GIC

Crystal Structure Of a Putative Histidinol dehydrogenase (Target PSI-014034) from Methylococcus capsulatus

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	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0008652	biological_process	amino acid biosynthetic process
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	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0008652	biological_process	amino acid biosynthetic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	ARG131
A	ARG210

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	ARG131
B	ARG210
B	HOH623

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Functional Information from PROSITE/UniProt

site_id	PS00611
Number of Residues	33
Details	HISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmv.AGPSEILVISdgrTdpdw..IAMDLFSqaEH

Chain	Residue	Details
A	ILE235-HIS267

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01024","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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