5ZLH
Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3
Summary for 5ZLH
| Entry DOI | 10.2210/pdb5zlh/pdb |
| Related | 5ZIS |
| Descriptor | Bifunctional cytochrome P450/NADPH--P450 reductase, MANGANESE PROTOPORPHYRIN IX (2 entities in total) |
| Functional Keywords | cytochrome p450, oxidoreductase |
| Biological source | Bacillus megaterium |
| Total number of polymer chains | 4 |
| Total formula weight | 211140.16 |
| Authors | Omura, K.,Aiba, Y.,Onoda, H.,Sugimoto, H.,Shoji, O.,Watanabe, Y. (deposition date: 2018-03-28, release date: 2018-08-15, Last modification date: 2024-03-27) |
| Primary citation | Omura, K.,Aiba, Y.,Onoda, H.,Stanfield, J.K.,Ariyasu, S.,Sugimoto, H.,Shiro, Y.,Shoji, O.,Watanabe, Y. Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A. Chem. Commun. (Camb.), 54:7892-7895, 2018 Cited by PubMed Abstract: Haem substitution is an effective approach to tweak the function of haemoproteins. Herein, we report a facile haem substitution method for self-sufficient cytochrome P450BM3 (CYP102A1) from Bacillus megaterium utilising the transpeptidase Sortase A from Staphylococcus aureus. We successfully constructed Mn-substituted BM3 and investigated its catalytic activity. PubMed: 29845154DOI: 10.1039/c8cc02760a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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