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Structure paper

TitleStructural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner.
Journal, issue, pagesBiochemistry, Vol. 52, Page 6211-6218, Year 2013
Publish dateMay 22, 2012 (structure data deposition date)
AuthorsCedervall, P.E. / Hooper, A.B. / Wilmot, C.M.
External linksBiochemistry / PubMed:23952581
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-4fas:
Complex crystal structure of hydroxylamine oxidoreductase and NE1300 from Nitrosomonas europaea
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HEC:
HEME C

ChemComp-ISW:
{3,3'-[(9S)-8,13-diethenyl-3,7,12,17-tetramethyl-9,10-dihydroporphyrin-2,18-diyl-kappa~4~N~21~,N~22~,N~23~,N~24~]dipropanoato(2-)}iron

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-NO3:
NITRATE ION

ChemComp-HOH:
WATER

Source
  • nitrosomonas europaea (bacteria)
KeywordsOXIDOREDUCTASE / Hydroxylamine oxidation / Heme c binding

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