4GHH
Structure of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with 4-Nitrocatechol at 1.55 Ang resolution
Summary for 4GHH
Entry DOI | 10.2210/pdb4ghh/pdb |
Related | 4GHC 4GHD 4GHE 4GHF 4GHG |
Descriptor | Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, HEXAETHYLENE GLYCOL, ... (9 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 | 169448.77 |
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 (1.55 Å) |
Structure validation
Download full validation report