1i9w

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF THE 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136783 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spike glycoprotein E1 Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 42.62 KDa
Source organism: Semliki Forest virus
UniProt:
  • Canonical: P03315 (Residues: 816-1205; Coverage: 31%)
Sequence domains: Alphavirus E1 glycoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P6422
Unit cell:
a: 79.46Å b: 79.46Å c: 334.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.275 0.275 0.344