Structure of H200N variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with 4-nitrocatechol at 1.57 Ang resolution

Summary for 4Z6W

Related4Z6L 4Z6M 4Z6N 4Z6O 4Z6Q 4Z6R 4Z6S 4Z6T 4Z6U 4Z6V 4Z6Z 4Z6P
DescriptorHomoprotocatechuate 2,3-dioxygenase, FE (II) ION, HEXAETHYLENE GLYCOL, ... (8 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 molecular weight169539.25
Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2015-04-06, release date: 2015-08-26, Last modification date: 2020-01-01)
Primary citation
Kovaleva, E.G.,Rogers, M.S.,Lipscomb, J.D.
Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200.
Biochemistry, 54:5329-5339, 2015
PubMed: 26267790 (PDB entries with the same primary citation)
DOI: 10.1021/acs.biochem.5b00709
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.1703 0.1% 1.8% 1.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-12-02