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1K75

The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processL-histidine biosynthetic process
A0004399molecular_functionhistidinol dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000105biological_processL-histidine biosynthetic process
B0004399molecular_functionhistidinol dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
APRO236
AHOH2425
ASER237
AHIS262
AGLY263
APRO264
AASP265
ASER266
AHOH2075
AHOH2156

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 2002
ChainResidue
BPRO236
BSER237
BHIS262
BGLY263
BPRO264
BASP265
BSER266
BHOH2119
BHOH2287
BHOH2397

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2003
ChainResidue
BPRO249
BARG280
BHOH2010

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
APRO249
AARG280
AHOH2051
BARG287

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AGLU72
AILE165
AASN183
AHOH2118
AHOH2268

Functional Information from PROSITE/UniProt
site_idPS00611
Number of Residues33
DetailsHISOL_DEHYDROGENASE Histidinol dehydrogenase signature. IDmp.AGPSEVLVIAdsgAtpdf..VASDLLSqaEH
ChainResidueDetails
AILE230-HIS262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11842181
ChainResidueDetails
AGLU326
AHIS327
BGLU326
BHIS327

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11842181
ChainResidueDetails
ATYR130
BASN211
BGLN259
BHIS262
BASP360
BHIS419
AGLN188
AASN211
AGLN259
AHIS262
AASP360
AHIS419
BTYR130
BGLN188

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:11842181
ChainResidueDetails
ASER237
AHIS327
AGLU414
BSER237
BHIS327
BGLU414

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 741
ChainResidueDetails
AGLN259metal ligand
AHIS262metal ligand
AGLU326proton acceptor, proton donor
AHIS327proton acceptor, proton donor
AASP360metal ligand
AHIS419metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 741
ChainResidueDetails
BGLN259metal ligand
BHIS262metal ligand
BGLU326proton acceptor, proton donor
BHIS327proton acceptor, proton donor
BASP360metal ligand
BHIS419metal ligand

225946

PDB entries from 2024-10-09

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