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Structure paper

TitleRoles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 6472-6481, Year 2020
Publish dateJan 22, 2020 (structure data deposition date)
AuthorsMamounis, K.J. / Yukl, E.T. / Davidson, V.L.
External linksJ. Biol. Chem. / PubMed:32234764
MethodsX-ray diffraction
Resolution1.99 - 2.24 Å
Structure data

PDB-6vl7:
Crystal structure of the H583C mutant of GoxA soaked with glycine
Method: X-RAY DIFFRACTION / Resolution: 2.14 Å

PDB-6vmf:
Crystal structure of the Y766F mutant of GoxA soaked with glycine
Method: X-RAY DIFFRACTION / Resolution: 2.24 Å

PDB-6vmv:
Crystal structure of the H767A mutant of GoxA soaked with glycine
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6vmw:
Crystal structure of the F316A mutant of GoxA soaked with glycine
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • pseudoalteromonas luteoviolacea dsm 6061 (bacteria)
KeywordsOXIDOREDUCTASE / CTQ

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