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TitlePorphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues
Journal, issue, pagesJ. Mol. Biol., Vol. 378, Page 1074-1083, Year 2008
Publish dateMay 29, 2007 (structure data deposition date)
AuthorsKarlberg, T. / Hansson, M.D. / Yengo, R.K. / Johansson, R. / Thorvaldsen, O.H. / Ferreira, G.C. / Hansson, M. / Al-Karadaghi, S.
External linksJ. Mol. Biol. / PubMed:18423489
MethodsX-ray diffraction
Resolution1.8 - 2.39 Å
Structure data

PDB-2q2n:
Crystal structure of Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2q2o:
Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2q3j:
Crystal structure of the His183Ala variant of Bacillus subtilis ferrochelatase in complex with N-Methyl Mesoporphyrin
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-H01:
PROTOPORPHYRIN IX 2,4-DISULFONIC ACID

ChemComp-HOH:
WATER

ChemComp-H02:
N-METHYL PROTOPORPHYRIN IX 2,4-DISULFONIC ACID

Source
  • bacillus subtilis (bacteria)
KeywordsTRANSFERASE / ROSSMANN FOLD; PI-HELIX / LYASE / ROSSMANN FOLD; PI-HELIX; N-METHYL MESOPORPHYRIN IX; N-MeMP

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