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-Structure paper
Title | Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis |
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Journal, issue, pages | Biochemistry, Vol. 46, Page 7973-7979, Year 2007 |
Publish date | Apr 24, 2007 (structure data deposition date) |
Authors | Dailey, H.A. / Wu, C.-K. / Horanyi, P. / Medlock, A.E. / Najahi-Missaoui, W. / Burden, A.E. / Dailey, T.A. / Rose, J.P. |
External links | Biochemistry / PubMed:17567154 |
Methods | X-ray diffraction |
Resolution | 2.2 - 2.35 Å |
Structure data | PDB-2pnj: PDB-2po5: PDB-2po7: |
Chemicals | ChemComp-FES: ChemComp-CHD: ChemComp-HOH: |
Source |
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Keywords | LYASE / FERROCHELATASE; F337A Mutant; FE2S2 CLUSTER; HEME BIOSYNTHESIS; PROTOHEME FERRO-LYASE; MATURE LENGTH; PROTEOLYTICALLY PROCESSED MITOCHONDRIAL INNER MEMBRANE PROTEIN / FERROCHELATASE; H263C; FE2S2 CLUSTER; HEME BIOSYNTHESIS; PROTOHEME; FERRO-LYASE; MATURE LENGTH; PROTEOLYTICALLY PROCESSED MITOCHONDRIAL INNER MEMBRANE PROTEIN / FERROCHELATASE; H341C; FE2S2 CLUSTER; HEME BIOSYNTHESIS; PROTOHEME; FERRO-LYASE; MATURE LENGTH; PROTEOLYTICALLY PROCESSED MITOCHONDRIAL INNER MEMBRANE PROTEIN |