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4GIC

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine 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_processhistidine 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 PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG131
AARG210

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG131
BARG210
BHOH623

Functional Information from PROSITE/UniProt
site_idPS00611
Number of Residues33
DetailsHISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmv.AGPSEILVISdgrTdpdw..IAMDLFSqaEH
ChainResidueDetails
AILE235-HIS267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01024
ChainResidueDetails
AGLU332
AHIS333
BGLU332
BHIS333

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01024
ChainResidueDetails
AHIS333
AASP366
AGLU420
BTYR135
BGLN196
BASN219
BSER242
BGLN264
BHIS267
BHIS333
BASP366
BGLU420
ATYR135
AGLN196
AASN219
ASER242
AGLN264
AHIS267

219869

PDB entries from 2024-05-15

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