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Structure paper

TitleThe Role of Selenocysteine in Catalysis and Oxygen Tolerance of a W‐Dependent Formate Dehydrogenase
Journal, issue, pagesAcs Catalysis, Year 2025
Publish dateMar 21, 2025 (structure data deposition date)
AuthorsOliveira, A.R. / Vilela-Alves, G. / Mota, C. / Fourmond, V. / Leger, C. / Biaso, F. / Guigliarelli, B. / Romao, M.J. / Pereira, I.C.
External linksAcs Catalysis / Search PubMed
MethodsX-ray diffraction
Resolution1.833 - 1.997 Å
Structure data

PDB-9qm0:
W-formate dehydrogenase U192C from Desulfovibrio vulgaris
Method: X-RAY DIFFRACTION / Resolution: 1.833 Å

PDB-9qm1:
W-formate dehydrogenase U192C from Desulfovibrio vulgaris - Soaked with Dithionite
Method: X-RAY DIFFRACTION / Resolution: 1.997 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-H2S:
HYDROSULFURIC ACID

ChemComp-W:
Unknown entry

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-HOH:
WATER

ChemComp-SO2:
SULFUR DIOXIDE

Source
  • nitratidesulfovibrio vulgaris str. hildenborough (bacteria)
KeywordsOXIDOREDUCTASE / Formate / CO2 / Molybdenum and Tungsten enzymes / DMSO reductase family / ELECTRON TRANSPORT

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