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TitleArchaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies.
Journal, issue, pagesPlos One, Vol. 11, Page e0147333-e0147333, Year 2016
Publish dateMay 6, 2015 (structure data deposition date)
AuthorsWakagi, T. / Nishimasu, H. / Miyake, M. / Fushinobu, S.
External linksPlos One / PubMed:26808202
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-4zoh:
Crystal structure of glyceraldehyde oxidoreductase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MCN:
PTERIN CYTOSINE DINUCLEOTIDE

ChemComp-MO:
MOLYBDENUM ATOM

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-ACY:
ACETIC ACID

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-HOH:
WATER

Source
  • sulfolobus tokodaii (strain dsm 16993 / jcm 10545 / nbrc 100140 / 7) (archaea)
KeywordsOXIDOREDUCTASE / xanthine oxidoreductase family / molybdopterin cofactor / flavin adenine dinucleotide / iron-sulfur cluster

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