3f6q

X-ray diffraction
1.6Å resolution

Crystal structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1 LIM1 domain

Released:
Source organism: Homo sapiens
Primary publication:
The structural basis of integrin-linked kinase-PINCH interactions.
Proc. Natl. Acad. Sci. U.S.A. 105 20677-82 (2008)
PMID: 19074270

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
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 1 Chain: B
Molecule details ›
Chain: B
Length: 72 amino acids
Theoretical weight: 8.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48059 (Residues: 6-68; Coverage: 19%)
Gene names: LIMS1, PINCH, PINCH1
Sequence domains: LIM domain
Structure domains: Cysteine Rich Protein

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 37.004Å b: 41.5Å c: 46.469Å
α: 78.01° β: 68.98° γ: 85.91°
R-values:
R R work R free
0.163 0.161 0.199
Expression system: Escherichia coli