5BWG
Structure of H200C variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.75 Ang resolution
Summary for 5BWG
Entry DOI | 10.2210/pdb5bwg/pdb |
Related | 5BWH |
Descriptor | Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, CHLORIDE ION, ... (7 entities in total) |
Functional Keywords | dioxygenase, 2-his-1-carboxylate facial triad, oxygen activation, acid-base catalysis, oxidoreductase |
Biological source | Brevibacterium fuscum |
Total number of polymer chains | 4 |
Total formula weight | 169325.98 |
Authors | Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2015-06-08, release date: 2015-10-28, Last modification date: 2023-09-27) |
Primary citation | Meier, K.K.,Rogers, M.S.,Kovaleva, E.G.,Mbughuni, M.M.,Bominaar, E.L.,Lipscomb, J.D.,Munck, E. A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mossbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorg.Chem., 54:10269-10280, 2015 Cited by PubMed: 26485328DOI: 10.1021/acs.inorgchem.5b01576 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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