H-Ras PEG 400/CaCl2, ordered off
The structure was published by Holzapfel, G., Buhrman, G., and Mattos, C., in 2012 in a paper entitled "Shift in the Equilibrium between On and Off States of the Allosteric Switch in Ras-GppNHp Affected by Small Molecules and Bulk Solvent Composition." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.391 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of GTPase HRas. This molecule has the UniProt identifier P20171 (RASH_RAT). The sample contained 166 residues which is < 90% of the natural sequence. Out of 166 residues 164 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 homohexamers.
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: