Crystal structure of the catalase-peroxidase from B. pseudomallei treated with acetate

Summary for 5KSK

Related5KQ0 5KQ2 5KQ3 5KQ6 5KQ7 5KQH 5KQI 5KQK 5KQN 5KQQ 5KSF 5KSG 5KSN 5KT8 5KT9
DescriptorCatalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (7 entities in total)
Functional Keywordscatalase, peroxidase, acetate, heme, oxidoreductase
Biological sourceBurkholderia pseudomallei (strain 1710b)
Total number of polymer chains2
Total molecular weight161142.7
Loewen, P.C. (deposition date: 2016-07-08, release date: 2017-04-26, Last modification date: 2017-09-27)
Primary citation
Machuqueiro, M.,Victor, B.,Switala, J.,Villanueva, J.,Rovira, C.,Fita, I.,Loewen, P.C.
The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.
Biochemistry, 56:2271-2281, 2017
PubMed: 28409923 (PDB entries with the same primary citation)
DOI: 10.1021/acs.biochem.6b01276
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.189301.9%1.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution