PDBe 1y64

X-ray diffraction
3.05Å resolution

Bni1p Formin Homology 2 Domain complexed with ATP-actin

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Protein BNI1 Chain: B
Molecule details ›
Chain: B
Length: 443 amino acids
Theoretical weight: 50.92 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P41832 (Residues: 1327-1769; Coverage: 23%)
Gene names: BNI1, N0646, PPF3, SHE5, YNL271C
Sequence domains: Formin Homology 2 Domain
Structure domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 231.997Å b: 56.229Å c: 100.945Å
α: 90° β: 107.7° γ: 90°
R-values:
R R work R free
0.313 0.289 0.313
Expression system: Escherichia coli