1rer

X-ray diffraction
3.2Å resolution

Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.

Released:

Function and Biology Details

Reaction catalysed:
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-136786 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Spike glycoprotein E1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 391 amino acids
Theoretical weight: 42.69 KDa
Source organism: Semliki Forest virus
UniProt:
  • Canonical: P03315 (Residues: 816-1206; Coverage: 31%)
Sequence domains: Alphavirus E1 glycoprotein
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, FUL
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer : NEW Components: NAG
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 198.197Å b: 198.197Å c: 116.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.266 0.265 0.285