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8XSQ

Pseudomonas aeruginosa Histidinol dehydrogenase native structure without Zn+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0004399molecular_functionhistidinol dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000105biological_processL-histidine biosynthetic process
B0004399molecular_functionhistidinol dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00611
Number of Residues33
DetailsHISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmi.AGPSEILVVCdgqTdpdw..IAMDLFSqaEH
ChainResidueDetails
AILE236-HIS268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01024","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01024","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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