1wyx Summary


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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CRK-associated substrate P56945 (3-71) (BCAR1_HUMAN)search Homo sapienssearch < 90% 69 100%
B CRK-associated substrate P56945 (3-71) (BCAR1_HUMAN)search Homo sapienssearch < 90% 69 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P56945 (3 - 71) CRK-associated substrate Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B SH3 Domainssearch SH3 domainsearch

Chain ID Molecular function (GO)
A, B (P56945) signal transducer activitysearch

Chain InterPro annotation
A, B SH3 domainsearch Spectrin alpha chain, SH3 domainsearch Breast cancer anti-estrogen resistance protein 1search