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TitleBarley Aldose Reductase: Structure, Cofactor Binding, and Substrate Recognition in the Aldo/Keto Reductase 4C Family.
Journal, issue, pagesProteins: Struct. , Funct. , Bioinf., Vol. 71, Page 1572-, Year 2008
Publish dateJan 4, 2005 (structure data deposition date)
AuthorsOlsen, J.G. / Pedersen, L. / Christensen, C.L. / Olsen, O. / Henriksen, A.
External linksProteins: Struct. , Funct. , Bioinf. / PubMed:18300247
MethodsX-ray diffraction
Resolution1.64 - 2.5 Å
Structure data

PDB-2bgq:
apo aldose reductase from barley
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-2bgs:
HOLO ALDOSE REDUCTASE FROM BARLEY
Method: X-RAY DIFFRACTION / Resolution: 1.64 Å

PDB-2vdg:
Barley Aldose Reductase 1 complex with butanol
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-1BO:
1-BUTANOL

Source
  • hordeum vulgare (barley)
KeywordsOXIDOREDUCTASE / ALDOSE REDUCTASE / APOENZYME / ALDO/KETO REDUCTASE OXIDOREDUCTASE / HOLOENZYME / ALDO/KETO REDUCTASE / STRESS RESPONSE / ALDO-KETO REDUCTASE / NADP / AKR4C / LIGAND COMPLEX

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