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5BWG

Structure of H200C variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.75 Ang resolution

Summary for 5BWG
Entry DOI10.2210/pdb5bwg/pdb
Related5BWH
DescriptorHomoprotocatechuate 2,3-dioxygenase, FE (II) ION, CHLORIDE ION, ... (7 entities in total)
Functional Keywordsdioxygenase, 2-his-1-carboxylate facial triad, oxygen activation, acid-base catalysis, oxidoreductase
Biological sourceBrevibacterium fuscum
Total number of polymer chains4
Total formula weight169325.98
Authors
Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2015-06-08, release date: 2015-10-28, Last modification date: 2023-09-27)
Primary citationMeier, 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: 26485328
DOI: 10.1021/acs.inorgchem.5b01576
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

218853

数据于2024-04-24公开中

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