1CKA: C-crk N-terminal SH3 domain

Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of C-crk. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 May 1995.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Mus musculus
Chains
2
Atoms
664
Mol. weight
7.92 kDa
Released
8 May 1995

Explore 1CKA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CKA contains 2 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 8 β-strands

ElementResiduesLengthSheet
β-strand136-13941
β-strand14312
β-strand15011
β-strand15312
β-strand158-16361
β-strand169-17351
β-strand179-18351
α-helix184-1863
β-strand187-18821
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
C-crk N-terminal SH3 domainAprotein57Mus musculusQ64010 (AlphaFold model)
C3G peptide (pro-pro-pro-ala-leu-pro-pro-lys-lys-arg)Bprotein10
Sequence of entity 1 (A), FASTA
>1CKA_1 C-CRK N-TERMINAL SH3 DOMAIN (chains A)
AEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKY
Sequence of entity 2 (B), FASTA
>1CKA_2 C3G PEPTIDE (PRO-PRO-PRO-ALA-LEU-PRO-PRO-LYS-LYS-ARG) (chains B)
PPPALPPKKR

Primary citation

Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Wu, X., Knudsen, B., Feller, S.M. et al. Structure (1995) 3:215-226. DOI 10.1016/S0969-2126(01)00151-4 · PubMed

Other PDB entries of the same protein (UniProt Q64010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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