4GHG

Structure of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with HPCA at 1.50 Ang resolution

Summary for 4GHG

Entry DOI	10.2210/pdb4ghg/pdb
Related	4GHC 4GHD 4GHE 4GHF 4GHH
Descriptor	Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, HEXAETHYLENE GLYCOL, ... (8 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	169359.35
Authors	Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2012-08-07, release date: 2012-10-31, Last modification date: 2024-02-28)
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: 23066739 DOI: 10.1021/bi301115c PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation