› 4bbk

X-ray diffraction
2.1Å resolution

Structural and functional characterisation of the kindlin-1 pleckstrin homology domain

Released:
DOI: 10.2210/pdb4bbk/pdb
PDB entry 4bbk coloured by chain, front view.
PDB entry 4bbk coloured by chain, side view.
PDB entry 4bbk coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural and functional characterization of the kindlin-1 pleckstrin homology domain.
Yates LA, Lumb CN, Brahme NN, Zalyte R, Bird LE, De Colibus L, Owens RJ, Calderwood DA, Sansom MS, Gilbert RJ
J Biol Chem 287 43246-61 (2012)
PMID: 23132860

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157775 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fermitin family homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.87 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P59113 (Residues: 364-509; Coverage: 22%)
Gene names: Fermt1, Kind1, Urp1
Sequence domains:
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 45.29Å b: 82.78Å c: 95.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Talins and kindlins: partners in integrin-mediated adhesion.
Calderwood et al. (2013)
5 more

4 mentions without citation

Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.
Ni et al. (2017)
3 more