Crystal Structure of the Human Beta2-Chimaerin
The structure was published by Canagarajah, B., Leskow, F.C., Ho, J.Y., et al., Saidi, L.F., Kazanietz, M.G., and Hurley, J.H., in 2004 in a paper entitled "Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.2 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Beta2-chimaerin. This molecule has the UniProt identifier P52757 (CHIO_HUMAN). The sample contained 466 residues which is 99% of the natural sequence. Out of 466 residues 398 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 is most likely monomeric.
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: