1TQJ
Crystal structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 angstrom resolution
Summary for 1TQJ
| Entry DOI | 10.2210/pdb1tqj/pdb |
| Descriptor | Ribulose-phosphate 3-epimerase (2 entities in total) |
| Functional Keywords | beta-alpha barrel epimerase, isomerase |
| Biological source | Synechocystis sp. |
| Total number of polymer chains | 6 |
| Total formula weight | 149986.82 |
| Authors | Wise, E.L.,Akana, J.,Gerlt, J.A.,Rayment, I. (deposition date: 2004-06-17, release date: 2004-08-31, Last modification date: 2024-02-14) |
| Primary citation | Wise, E.L.,Akana, J.,Gerlt, J.A.,Rayment, I. Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution. Acta Crystallogr.,Sect.D, 60:1687-1690, 2004 Cited by PubMed Abstract: The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 A resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (beta/alpha)(8)-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues. PubMed: 15333955DOI: 10.1107/S0907444904015896 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
