3ixe

X-ray diffraction
1.9Å resolution

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Integrin-linked protein kinase Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 20.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13418 (Residues: 1-174; Coverage: 39%)
Gene names: ILK, ILK1, ILK2
Sequence domains:
Structure domains: Ankyrin repeat-containing domain
LIM and senescent cell antigen-like-containing domain protein 2 Chain: B
Molecule details ›
Chain: B
Length: 72 amino acids
Theoretical weight: 8.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7Z4I7 (Residues: 11-73; Coverage: 19%)
Gene names: LIMS2, PINCH2
Sequence domains: LIM domain
Structure domains: Cysteine Rich Protein

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 41.416Å b: 72.01Å c: 83.937Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.22
Expression system: Escherichia coli BL21