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4IJC

Crystal structure of arabinose dehydrogenase Ara1 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004032molecular_functionaldose reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0045149biological_processacetoin metabolic process
A0045290molecular_functionD-arabinose 1-dehydrogenase [NAD(P)+] activity
A0047816molecular_functionD-arabinose 1-dehydrogenase (NAD+) activity
A0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
A0106271molecular_functionD-arabinose 1-dehydrogenase (NADP+) activity
B0004032molecular_functionaldose reductase (NADPH) activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0045149biological_processacetoin metabolic process
B0045290molecular_functionD-arabinose 1-dehydrogenase [NAD(P)+] activity
B0047816molecular_functionD-arabinose 1-dehydrogenase (NAD+) activity
B0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
B0106271molecular_functionD-arabinose 1-dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
ASER241
ASER245
AARG285
ASO4402
AHOH530
AHOH628

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AGLY244
AARG285
ASO4401
AHOH629
ASER241
APRO242
ALEU243

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AVAL31
AARG187
AHOH637
AHOH665
BLYS91
BHOH628

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BSER241
BPRO242
BLEU243
BGLY244
BSER245
BARG285
BSO4402
BHOH552
BHOH592
BHOH634

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BSER241
BSER245
BARG285
BSO4401

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. IyldpndhrVRAIGVSNF
ChainResidueDetails
AILE177-PHE194

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPRSLNpvRIsSSiEF
ChainResidueDetails
AILE283-PHE298

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAwayetEpfVG
ChainResidueDetails
AGLY61-GLY78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues110
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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