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Structure paper

TitleAmino Acid Residues His183 and Glu264 in Bacillus subtilis Ferrochelatase Direct and Facilitate the Insertion of Metal Ion into Protoporphyrin IX
Journal, issue, pagesBiochemistry, Vol. 46, Page 87-94, Year 2007
Publish dateMay 17, 2006 (structure data deposition date)
AuthorsHansson, M.D. / Karlberg, T. / Rahardja, M.A. / Al-Karadaghi, S. / Hansson, M.
External linksBiochemistry / PubMed:17198378
MethodsX-ray diffraction
Resolution1.2 - 2.6 Å
Structure data

PDB-2h1v:
Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-2h1w:
Crystal structure of the His183Ala mutant variant of Bacillus subtilis ferrochelatase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-2hk6:
Crystal Structure of B. subtilis ferrochelatase with Iron bound at the active site
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FE2:
Unknown entry

ChemComp-FE:
Unknown entry

Source
  • bacillus subtilis (bacteria)
KeywordsLYASE / ROSSMANN FOLD / PI-HELIX / Heme biosynthesis / Iron / Metal-binding / Porphyrin biosynthesis

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