8V37

Crystal structure of HpsN D352A mutant from Cupriavidus pinatubonensis in complex with NAD+

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	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	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 PROSITE/UniProt

site_id	PS00611
Number of Residues	33
Details	HISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDvf.AGPSEVAVIAdetAdpai..VASDLVGqaEH

Chain	Residue	Details
A	ILE219-HIS251

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P06988","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02228","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P06988","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02228","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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