2CKF
Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1
Summary for 2CKF
| Entry DOI | 10.2210/pdb2ckf/pdb |
| Descriptor | RING-HYDROXYLATING DIOXYGENASE ALPHA SUBUNIT, RING-HYDROXYLATING DIOXYGENASE BETA SUBUNIT, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total) |
| Functional Keywords | rieske non heme iron dioxygenase, pyrene dioxygenase, ring-hydroxylating dioxygenase, high-molecular-weight polycyclic aromatic hydrocarbons, oxidoreductase |
| Biological source | SPHINGOMONAS SP. More |
| Total number of polymer chains | 6 |
| Total formula weight | 215737.76 |
| Authors | Jakoncic, J.,Meyer, C.,Jouanneau, Y.,Stojanoff, V. (deposition date: 2006-04-18, release date: 2007-01-02, Last modification date: 2024-05-01) |
| Primary citation | Jakoncic, J.,Jouanneau, Y.,Meyer, C.,Stojanoff, V. The Catalytic Pocket of the Ring-Hydroxylating Dioxygenase from Sphingomonas Chy-1. Biochem.Biophys.Res.Commun., 352:861-, 2007 Cited by PubMed Abstract: Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme. PubMed: 17157819DOI: 10.1016/J.BBRC.2006.11.117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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