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TitleUltrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism.
Journal, issue, pagesJ. Inorg. Biochem., Vol. 104, Page 683-690, Year 2010
Publish dateMar 12, 2010 (structure data deposition date)
AuthorsSundaramoorthy, M. / Gold, M.H. / Poulos, T.L.
External linksJ. Inorg. Biochem. / PubMed:20356630
MethodsX-ray diffraction
Resolution0.93 - 1.05 Å
Structure data

PDB-3m5q:
0.93 A Structure of Manganese-Bound Manganese Peroxidase
Method: X-RAY DIFFRACTION / Resolution: 0.93 Å

PDB-3m8m:
1.05 A Structure of Manganese-free Manganese Peroxidase
Method: X-RAY DIFFRACTION / Resolution: 1.05 Å

Chemicals

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-CA:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

Source
  • phanerochaete chrysosporium (fungus)
KeywordsOXIDOREDUCTASE / Peroxidase / Heme / Mn(II)-binding site / Ca(II)-binding site / Glycosylation / Ultrahigh resolution / Calcium / Disulfide bond / Glycoprotein / Hydrogen peroxide / Iron / Lignin degradation / Manganese / Metal-binding / Secreted / high resolution

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