1ZOA
Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine
Summary for 1ZOA
Entry DOI | 10.2210/pdb1zoa/pdb |
Related | 1BU7 1JPZ 1ZO4 1ZO9 2HPD |
Descriptor | Bifunctional P-450:NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, N-PALMITOYLGLYCINE, ... (6 entities in total) |
Functional Keywords | cytochrome p-450, hemeprotein a328v, oxidoreductase |
Biological source | Bacillus megaterium |
Cellular location | Cytoplasm (By similarity): P14779 |
Total number of polymer chains | 2 |
Total formula weight | 110287.53 |
Authors | Hegda, A.,Chen, B.,Haines, D.C.,Bondlela, M.,Mullin, D.,Graham, S.E.,Tomchick, D.R.,Machius, M.,Peterson, J.A. (deposition date: 2005-05-12, release date: 2006-08-01, Last modification date: 2023-08-23) |
Primary citation | Haines, D.C.,Hegde, A.,Chen, B.,Zhao, W.,Bondlela, M.,Humphreys, J.M.,Mullin, D.A.,Tomchick, D.R.,Machius, M.,Peterson, J.A. A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation. Biochemistry, 50:8333-8341, 2011 Cited by PubMed: 21875028DOI: 10.1021/bi201099j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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