› 5l81

X-ray diffraction
2.23Å resolution

Crystal structure of the PH domain of murine kindlin-3

Released:
DOI: 10.2210/pdb5l81/pdb
PDB entry 5l81 coloured by chain, front view.
PDB entry 5l81 coloured by chain, side view.
PDB entry 5l81 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.
Ni T, Kalli AC, Naughton FB, Yates LA, Naneh O, Kozorog M, Anderluh G, Sansom MS, Gilbert RJ
Biochem J 474 539-556 (2017)
PMID: 27974389

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-185048 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fermitin family homolog 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 150 amino acids
Theoretical weight: 16.89 KDa
Source organism: Mus musculus
Expression system: Escherichia coli B
UniProt:
  • Canonical: Q8K1B8 (Residues: 344-478; Coverage: 20%)
Gene names: Fermt3, Kind3, Urp2
Sequence domains:
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P21212
Unit cell:
a: 132.04Å b: 36.19Å c: 52.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.271
Expression system: Escherichia coli B

Quick links

Citations

9 review citations

Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.
Muller et al. (2019)
8 more

2 mentions without citation

Structural basis of human full-length kindlin-3 homotrimer in an auto-inhibited state.
Bu et al. (2020)
1 more