4GHE
Structure of Y257F variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with 4-nitrocatechol at 1.60 Ang resolution
Summary for 4GHE
Entry DOI | 10.2210/pdb4ghe/pdb |
Related | 4GHC 4GHD 4GHF 4GHG 4GHH |
Descriptor | Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, HEXAETHYLENE GLYCOL, ... (7 entities in total) |
Functional Keywords | dioxygenase, oxygen activation, fe(ii), 2-his-1-carboxylate facial triad, homoprotocatechuate, 4-nitrocatechol, oxy complex, oxidoreductase |
Biological source | Brevibacterium fuscum |
Total number of polymer chains | 4 |
Total formula weight | 169493.98 |
Authors | Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2012-08-07, release date: 2012-10-31, Last modification date: 2023-09-13) |
Primary citation | Kovaleva, E.G.,Lipscomb, J.D. Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry, 51:8755-8763, 2012 Cited by PubMed: 23066739DOI: 10.1021/bi301115c PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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