6DCD
Mycobacterium marinum cytochrome P450 CYP150A6 in the substrate-free form
Summary for 6DCD
| Entry DOI | 10.2210/pdb6dcd/pdb |
| Descriptor | Cytochrome P450 150A6 Cyp150A6, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450, monooxygenase, heme protein, oxidoreductase |
| Biological source | Mycobacterium marinum |
| Total number of polymer chains | 1 |
| Total formula weight | 48395.29 |
| Authors | Child, S.A.,Bruning, J.B.,Bell, S.G. (deposition date: 2018-05-05, release date: 2019-03-20, Last modification date: 2024-03-13) |
| Primary citation | Child, S.A.,Flint, K.L.,Bruning, J.B.,Bell, S.G. The characterisation of two members of the cytochrome P450 CYP150 family: CYP150A5 and CYP150A6 from Mycobacterium marinum. Biochim Biophys Acta Gen Subj, 1863:925-934, 2019 Cited by PubMed Abstract: Actinobacteria, including the Mycobacteria, have a large component of cytochrome P450 family monooxygenases. This includes Mycobacterium tuberculosis, M. ulcerans and M. marinum, and M. vanbaalenii. These enzymes can abstract CH bonds and have important roles in natural product biosynthesis. PubMed: 30826435DOI: 10.1016/j.bbagen.2019.02.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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