1ckb Summary

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STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK

The structure was published by Wu, X., Knudsen, B., Feller, S.M., et al., Cowburn, D., Hanafusa, H., and Kuriyan, J., in 1995 in a paper entitled "Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1995.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely C-CRK N-TERMINAL SH3 DOMAIN and SOS PEPTIDE (PRO-PRO-PRO-VAL-PRO-PRO-ARG-ARG-ARG-ARG).

The molecule most likely forms heterodimers.

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 C-CRK N-TERMINAL SH3 DOMAIN Q64010 (134-190) (CRK_MOUSE)search Mus musculussearch < 90% 57 100%
B SOS PEPTIDE (PRO-PRO-PRO-VAL-PRO-PRO-ARG-ARG-ARG-ARG) Not available
Homo sapienssearch Not available 10 80%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q64010 (134 - 190) C-CRK N-TERMINAL SH3 DOMAIN Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A SH3-domainsearch SH3 Domainssearch SH3 domainsearch
B
Chain InterPro annotation
A SH3 domainsearch
B