2J27

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

Summary for 2J27

Related1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 3TIM 4TIM 5TIM 6TIM 2J24
DescriptorTRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, ... (4 entities in total)
Functional Keywordstim, 2pg, loop7, isomerase, glycosome, tim-barrel, gluconeogenesis, lipid synthesis, atomic resolution, glycolysis, pentose shunt, point mutation, fatty acid biosynthesis, 2-phospho glycolate, protein engineering
Biological sourceTRYPANOSOMA BRUCEI BRUCEI
Total number of polymer chains2
Total molecular weight54087.72
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: 2019-07-24)
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 (1.15 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.14440 1.8% 1.0%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