The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution
The structure was published by Wisniewska, M., Bossenmaier, B., Georges, G., et al., Ioannidis, I., Huber, R., and Engh, R.A., in 2005 in a paper entitled "The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.14 Å and deposited in 2005.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of CRK-associated substrate.
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: