Summary for 2VO1
| Entry DOI | 10.2210/pdb2vo1/pdb |
| Related | 2C5M |
| Descriptor | CTP SYNTHASE 1, SULFATE ION (3 entities in total) |
| Functional Keywords | pyrimidine biosynthesis, glutamine amidotransferase, phosphorylation, amidotransferase, cytidine 5-prime triphosphate synthetase, ctp, utp, ctps, ligase, glutamine, ctp synthase, phosphoprotein, ctp synthetase |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 66521.60 |
| Authors | Stenmark, P.,Kursula, P.,Arrowsmith, C.,Berglund, H.,Edwards, A.,Ehn, M.,Flodin, S.,Graslund, S.,Hammarstrom, M.,Hallberg, B.M.,Holmberg-Schiavone, L.,Kotenyoa, T.,Moche, M.,Nilsson-Ehle, P.,Ogg, D.,Persson, C.,Sagemark, J.,Schuler, H.,Sundstrom, M.,Thorsell, A.G.,Van Den Berg, S.,Weigelt, J.,Nordlund, P. (deposition date: 2008-02-08, release date: 2008-03-11, Last modification date: 2024-11-13) |
| Primary citation | Kursula, P.,Flodin, S.,Ehn, M.,Hammarstrom, M.,Schuler, H.,Nordlund, P.,Stenmark, P. Structure of the Synthetase Domain of Human Ctp Synthetase, a Target for Anticancer Therapy. Acta Crystallogr.,Sect.F, 62:613-, 2006 Cited by PubMed Abstract: Cytidine triphosphate synthetase (CTPS) is a key enzyme in nucleic acid and phospholipid biosynthesis and its activity is increased in certain human cancers, making it a promising drug target. The crystal structure of the synthetase domain of human CTPS, which represents the first structure of a CTPS from an eukaryote, has been determined. The structure is homotetrameric and each active site is formed by three different subunits. Sulfate ions bound to the active sites indicate the positions of phosphate-binding sites for the substrates ATP and UTP and the feedback inhibitor CTP. Together with earlier structures of bacterial CTPS, the human CTPS structure provides an extended understanding of the structure-function relationship of CTPS-family members. The structure also serves as a basis for structure-based design of anti-proliferative inhibitors. PubMed: 16820675DOI: 10.1107/S1744309106018136 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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