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Structure paper

TitleHuman xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate
Journal, issue, pagesJ. Biochem. (Tokyo), Vol. 141, Page 513-524, Year 2007
Publish dateOct 27, 2006 (structure data deposition date)
AuthorsYamaguchi, Y. / Matsumura, T. / Ichida, K. / Okamoto, K. / Nishino, T.
External linksJ. Biochem. (Tokyo) / PubMed:17301077
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-2e1q:
Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-CA:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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

ChemComp-MTE:
PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER

ChemComp-MOM:
HYDROXY(DIOXO)MOLYBDENUM

ChemComp-SAL:
2-HYDROXYBENZOIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / xanthine oxidase / molybdenum cofactor / FAD

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