2J27
The functional role of the conserved active site proline of triosephosphate isomerase.
Summary for 2J27
Entry DOI | 10.2210/pdb2j27/pdb |
Related | 1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 3TIM 4TIM 5TIM 6TIM |
Descriptor | TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, ... (4 entities in total) |
Functional Keywords | tim, 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 source | TRYPANOSOMA BRUCEI BRUCEI |
Total number of polymer chains | 2 |
Total formula weight | 54087.71 |
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: 2024-05-01) |
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 Cited by PubMed: 17176070DOI: 10.1021/BI061683J PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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