Summary for 3IXQ
| Entry DOI | 10.2210/pdb3ixq/pdb |
| Descriptor | Ribose-5-phosphate isomerase A, CHLORIDE ION, S-1,2-PROPANEDIOL, ... (5 entities in total) |
| Functional Keywords | structural genomics, isomerase, pentose phosphate pathway, carbon fixation, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, carbohydrate metabolism |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 4 |
| Total formula weight | 100477.24 |
| Authors | Antonyuk, S.V.,Ellis, M.J.,Strange, R.W.,Hasnain, S.S.,Bessho, Y.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-09-04, release date: 2009-10-06, Last modification date: 2023-11-01) |
| Primary citation | Strange, R.W.,Antonyuk, S.V.,Ellis, M.J.,Bessho, Y.,Kuramitsu, S.,Yokoyama, S.,Hasnain, S.S. The structure of an archaeal ribose-5-phosphate isomerase from Methanocaldococcus jannaschii (MJ1603). Acta Crystallogr.,Sect.F, 65:1214-1217, 2009 Cited by PubMed Abstract: Ribose-5-phosphate isomerase is a ubiquitous intracellular enzyme of bacterial, plant and animal origin that is involved in the pentose phosphate cycle, an essential component of cellular carbohydrate metabolism. Specifically, the enzyme catalyses the reversible conversion of ribose 5-phosphate to ribulose 5-phosphate. The structure of ribose-5-phosphate isomerase from Methanocaldococcus jannaschii has been solved in space group P2(1) to 1.78 A resolution using molecular replacement with one homotetramer in the asymmetric unit and refined to an R factor of 14.8%. The active site in each subunit was occupied by two molecules of propylene glycol in different orientations, one of which corresponds to the location of the phosphate moiety and the other to the location of the furanose ring of the inhibitor. PubMed: 20054114DOI: 10.1107/S1744309109044923 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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