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-Structure paper
Title | Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. |
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Journal, issue, pages | J. Biol. Chem., Vol. 282, Page 564-572, Year 2007 |
Publish date | Sep 29, 2006 (structure data deposition date) |
![]() | Girvan, H.M. / Seward, H.E. / Toogood, H.S. / Cheesman, M.R. / Leys, D. / Munro, A.W. |
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Methods | X-ray diffraction |
Resolution | 1.2 - 2.4 Å |
Structure data | ![]() PDB-2ij2: ![]() PDB-2ij3: ![]() PDB-2ij4: |
Chemicals | ![]() ChemComp-HEM: ![]() ChemComp-HOH: |
Source |
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![]() | OXIDOREDUCTASE / Cytochrome P450 / P450BM3 / monoxygenase / heme binding protein / atomic resolution / heme ligation / histidine ligation / P450 BM3 / lysine heme ligation |