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

DescriptorC-H-RAS P21 PROTEIN, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
Functional Keywordsoncogene protein
Biological sourceHomo sapiens (human)
Cellular locationCell membrane. Isoform 2: Nucleus P01112
Total number of polymer chains1
Total molecular weight19421.69
Authors
Pai, E.F.,Wittinghofer, A.,Kabsch, W. (deposition date: 1990-04-30, release date: 1992-01-15, Last modification date: 2017-11-29)
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
PubMed: 2196171 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.35 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers20 2.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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171588
PDB entries from 2020-11-25