3zwg

X-ray diffraction
3Å resolution

Crystal structure of the pore-forming toxin FraC from Actinia fragacea (form 2)

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DELTA-actitoxin-Afr1a Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 179 amino acids
Theoretical weight: 19.75 KDa
Source organism: Actinia fragacea
UniProt:
  • Canonical: B9W5G6 (Residues: 1-179; Coverage: 100%)
Sequence domains: Sea anemone cytotoxic protein
Structure domains: Cytolysin/lectin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P312
Unit cell:
a: 118.77Å b: 118.77Å c: 431.822Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.25