REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS
The structure was published by Pai, E.F., Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W., and Wittinghofer, A., in 1990 in a paper entitled "Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.35 Å and deposited in 1990.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of C-H-RAS P21 PROTEIN. This molecule has the UniProt identifier P01112 (RASH_HUMAN). The sample contained 166 residues which is < 90% of the natural sequence. Out of 166 residues 166 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: