5P21
REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS
Summary for 5P21
Entry DOI | 10.2210/pdb5p21/pdb |
Descriptor | C-H-RAS P21 PROTEIN, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total) |
Functional Keywords | oncogene protein |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane. Isoform 2: Nucleus: P01112 |
Total number of polymer chains | 1 |
Total formula weight | 19421.69 |
Authors | Pai, E.F.,Wittinghofer, A.,Kabsch, W. (deposition date: 1990-04-30, release date: 1992-01-15, Last modification date: 2024-03-06) |
Primary citation | Pai, E.F.,Krengel, U.,Petsko, G.A.,Goody, R.S.,Kabsch, W.,Wittinghofer, A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J., 9:2351-2359, 1990 Cited by PubMed: 2196171PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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