4eah

X-ray diffraction
3.4Å resolution

Crystal structure of the formin homology 2 domain of FMNL3 bound to actin

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-159318 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chains: D, F, G, H
Molecule details ›
Chains: D, F, G, H
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Formin-like protein 3 Chains: A, B, C, E
Molecule details ›
Chains: A, B, C, E
Length: 402 amino acids
Theoretical weight: 46.01 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6ZPF4 (Residues: 555-954; Coverage: 39%)
Gene names: Fmnl3, Frl2, Kiaa2014
Sequence domains: Formin Homology 2 Domain
Structure domains: Formin, FH2 domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 125.98Å b: 126.05Å c: 129.62Å
α: 90° β: 93.17° γ: 90°
R-values:
R R work R free
0.232 0.23 0.277
Expression system: Escherichia coli BL21