5KYO
Crystal Structure of CYP101J2
Summary for 5KYO
| Entry DOI | 10.2210/pdb5kyo/pdb |
| Descriptor | CYP101J2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450 monooxygenase, 1, 8-cineole hydroxylation, oxidoreductase |
| Biological source | Sphingobium yanoikuyae |
| Total number of polymer chains | 6 |
| Total formula weight | 296245.07 |
| Authors | Unterweger, B.,Drinkwater, N.,Dumsday, G.J.,McGowan, S. (deposition date: 2016-07-22, release date: 2017-01-04, Last modification date: 2023-10-04) |
| Primary citation | Unterweger, B.,Drinkwater, N.,Johanesen, P.,Lyras, D.,Dumsday, G.J.,McGowan, S. X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2. Proteins, 85:945-950, 2017 Cited by PubMed Abstract: The cytochrome P450 monooxygenases (P450s) catalyze a vast array of oxygenation reactions that can be useful in biocatalytic applications. CYP101J2 from Sphingobium yanoikuyae is a P450 that catalyzes the hydroxylation of 1,8-cineole. Here we report the crystallization and X-ray structure elucidation of recombinant CYP101J2 to 1.8 Å resolution. The CYP101J2 structure shows the canonical P450-fold and has an open conformation in the absence of substrate. Analysis of the structure revealed that CYP101J2, in the absence of substrate, forms a well-ordered substrate-binding channel that suggests a unique form of substrate guidance in comparison to other bacterial 1,8-cineole-hydroxylating P450 enzymes. Proteins 2017; 85:945-950. © 2016 Wiley Periodicals, Inc. PubMed: 27936485DOI: 10.1002/prot.25227 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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