5ih2

X-ray diffraction
1.8Å resolution

Structure, thermodynamics, and the role of conformational dynamics in the interactions between the N-terminal SH3 domain of CrkII and proline-rich motifs in cAbl

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 58 amino acids
Theoretical weight: 6.97 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64010 (Residues: 134-191; Coverage: 19%)
Gene names: Crk, Crko
Sequence domains: SH3 domain
Structure domains: SH3 Domains
Tyrosine-protein kinase ABL1 Chains: M, N
Molecule details ›
Chains: M, N
Length: 12 amino acids
Theoretical weight: 1.29 KDa
Source organism: Endothia gyrosa
Expression system: Not provided
UniProt:
  • Canonical: P00520 (Residues: 757-765; Coverage: 1%)
Gene names: Abl, Abl1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 45.222Å b: 29.479Å c: 45.756Å
α: 90° β: 94.31° γ: 90°
R-values:
R R work R free
0.173 0.17 0.243
Expression systems:
  • Escherichia coli
  • Not provided