Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

Summary for 5I3F

Related5I3I 5I3J 5I3K 5I3G 5I3H
DescriptorTriosephosphate isomerase, glycosomal (2 entities in total)
Functional Keywordstriosephosphate isomerase, catalysis, hydrophobic clamping, isomerase
Biological sourceTrypanosoma brucei brucei
Cellular locationGlycosome P04789
Total number of polymer chains4
Total molecular weight107295.01
Drake, E.J.,Gulick, A.M.,Richard, J.P.,Zhai, X.,Kim, K.,Reinhardt, C.J. (deposition date: 2016-02-10, release date: 2016-05-18, Last modification date: 2016-06-15)
Primary citation
Richard, J.P.,Amyes, T.L.,Malabanan, M.M.,Zhai, X.,Kim, K.J.,Reinhardt, C.J.,Wierenga, R.K.,Drake, E.J.,Gulick, A.M.
Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55:3036-3047, 2016
PubMed: 27149328 (PDB entries with the same primary citation)
DOI: 10.1021/acs.biochem.6b00311
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.22620 0.3% 2.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-11-18