2fgh

X-ray diffraction
2.8Å resolution

ATP bound gelsolin

Released:
Source organism: Equus caballus
Primary publication:
The structure of gelsolin bound to ATP.
J Mol Biol 357 765-72 (2006)
PMID: 16469333

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-173310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gelsolin Chains: A, B
Molecule details ›
Chains: A, B
Length: 731 amino acids
Theoretical weight: 80.92 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: Q28372 (Residues: 2-731; Coverage: 100%)
Gene name: GSN
Sequence domains: Gelsolin repeat
Structure domains: Severin

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P4212
Unit cell:
a: 167.344Å b: 167.344Å c: 149.883Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.242 0.265