PDBe 1cka

X-ray diffraction
1.5Å resolution

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

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Adapter molecule crk Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64010 (Residues: 134-190; Coverage: 19%)
Gene names: Crk, Crko
Sequence domains: SH3 domain
Structure domains: SH3 Domains
C3G PEPTIDE (PRO-PRO-PRO-ALA-LEU-PRO-PRO-LYS-LYS-ARG) Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.1 KDa
Source organism: Unidentified
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 47.2Å b: 47.2Å c: 29.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression systems:
  • Escherichia coli
  • Not provided