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Structure paper

TitleThe crystal structure of the mutant K300M of polyamine oxidase from ZEA MAYS unveils the role of LYS300 in catalysis
Journal, issue, pagesTo be Published
Publish dateNov 16, 2009 (structure data deposition date)
AuthorsFiorillo, A. / Ilari, A. / Tavladoraki, P.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.9 - 3.2 Å
Structure data

PDB-3kpf:
X-ray structure of the mutant Lys300Met of polyamine oxidase from Zea mays
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-3ku9:
X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

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

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CL:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-SPM:
SPERMINE

Source
  • zea mays (maize)
KeywordsOXIDOREDUCTASE / FLAVOENZYME / POLYAMINE OXIDASE / Disulfide bond / FAD / Flavoprotein / Glycoprotein

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