2J24

The functional role of the conserved active site proline of triosephosphate isomerase

Summary for 2J24

Related1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 3TIM 4TIM 5TIM 6TIM
DescriptorTRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL (2 entities in total)
Functional Keywordsisomerase, protein engineering, fatty acid biosynthesis, gluconeogenesis, lipid synthesis, pentose shunt, point mutation, loop7, glycosome, tim-barrel
Biological sourceTRYPANOSOMA BRUCEI BRUCEI
Cellular locationGlycosome P04789
Total number of polymer chains2
Total molecular weight53679.59
Authors
Casteleijn, M.G.,Alahuhta, M.,Groebel, K.,El-Sayed, I.,Augustyns, K.,Lambeir, A.M.,Neubauer, P.,Wierenga, R.K. (deposition date: 2006-08-16, release date: 2007-01-02, Last modification date: 2017-06-28)
Primary citation
Casteleijn, M.G.,Alahuhta, M.,Groebel, K.,El-Sayed, I.,Augustyns, K.,Lambeir, A.M.,Neubauer, P.,Wierenga, R.K.
Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45:15483-, 2006
PubMed: 17176070 (PDB entries with the same primary citation)
DOI: 10.1021/BI061683J
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.23880 4.6% 0.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
171313
PDB entries from 2020-11-18