1O7G
NAPHTHALENE 1,2-DIOXYGENASE WITH NAPHTHALENE BOUND IN THE ACTIVE SITE.
Summary for 1O7G
| Entry DOI | 10.2210/pdb1o7g/pdb |
| Related | 1EG9 1NDO 1O7H 1O7M 1O7N 1O7P 1O7W |
| Descriptor | NAPHTHALENE 1,2-DIOXYGENASE ALPHA SUBUNIT, NAPHTHALENE 1,2-DIOXYGENASE BETA SUBUNIT, 1,2-ETHANEDIOL, ... (8 entities in total) |
| Functional Keywords | oxidoreductase, non-heme iron dioxygenase, enzyme-substrate complex, iron-sulfur, aromatic hydrocarbon catabolism |
| Biological source | PSEUDOMONAS PUTIDA More |
| Total number of polymer chains | 2 |
| Total formula weight | 73653.88 |
| Authors | Karlsson, A.,Parales, J.V.,Parales, R.E.,Gibson, D.T.,Eklund, H.,Ramaswamy, S. (deposition date: 2002-11-05, release date: 2003-02-20, Last modification date: 2023-12-13) |
| Primary citation | Karlsson, A.,Parales, J.V.,Parales, R.E.,Gibson, D.T.,Eklund, H.,Ramaswamy, S. Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron Science, 299:1039-, 2003 Cited by PubMed Abstract: Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase. PubMed: 12586937DOI: 10.1126/SCIENCE.1078020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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