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: 2196171 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.35 Å)

Structure validation