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| Title | Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis |
|---|---|
| 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 |
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homo sapiens (human)
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