PDBe 3eg1

X-ray diffraction
1.85Å resolution

Crystal structure of the N114Q mutant of ABL-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
p41 peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.04 KDa
Source organism: Synthetic construct
Expression system: Not provided
UniProt:
Tyrosine-protein kinase ABL1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 63 amino acids
Theoretical weight: 7.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00519 (Residues: 60-121; Coverage: 6%)
Gene names: ABL, ABL1, JTK7
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 45.996Å b: 47.636Å c: 55.662Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.185 0.248
Expression systems:
  • Not provided
  • Escherichia coli