1QRA
STRUCTURE OF P21RAS IN COMPLEX WITH GTP AT 100 K
Summary for 1QRA
| Entry DOI | 10.2210/pdb1qra/pdb |
| Descriptor | TRANSFORMING PROTEIN P21/H-RAS-1, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | g protein, gtp hydrolysis, kinetic crystallography, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane. Isoform 2: Nucleus: P01112 |
| Total number of polymer chains | 1 |
| Total formula weight | 19422.68 |
| Authors | Scheidig, A.,Burmester, C.,Goody, R.S. (deposition date: 1999-06-12, release date: 1999-11-05, Last modification date: 2023-08-16) |
| Primary citation | Scheidig, A.J.,Burmester, C.,Goody, R.S. The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure Fold.Des., 7:1311-1324, 1999 Cited by PubMed Abstract: In numerous biological events the hydrolysis of guanine triphosphate (GTP) is a trigger to switch from the active to the inactive protein form. In spite of the availability of several high-resolution crystal structures, the details of the mechanism of nucleotide hydrolysis by GTPases are still unclear. This is partly because the structures of the proteins in their active states had to be determined in the presence of non-hydrolyzable GTP analogues (e.g. GppNHp). Knowledge of the structure of the true Michaelis complex might provide additional insights into the intrinsic protein hydrolysis mechanism of GTP and related nucleotides. PubMed: 10574788DOI: 10.1016/S0969-2126(00)80021-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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