2yew

Electron Microscopy
5Å resolution

Modeling Barmah Forest virus structural proteins

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero 720-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161029 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein Chains: A, D, G, J
Molecule details ›
Chains: A, D, G, J
Length: 253 amino acids
Theoretical weight: 28.31 KDa
Source organism: Barmah Forest virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P89946 (Residues: 1-253; Coverage: 20%)
Sequence domains: Alphavirus core protein
Spike glycoprotein E1 Chains: B, E, H, K
Molecule details ›
Chains: B, E, H, K
Length: 427 amino acids
Theoretical weight: 46.28 KDa
Source organism: Barmah Forest virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P89946 (Residues: 801-1239; Coverage: 35%)
Sequence domains: Alphavirus E1 glycoprotein
Spike glycoprotein E2 Chains: C, F, I, L
Molecule details ›
Chains: C, F, I, L
Length: 421 amino acids
Theoretical weight: 46.19 KDa
Source organism: Barmah Forest virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P89946 (Residues: 322-742; Coverage: 34%)
Sequence domains: Alphavirus E2 glycoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution:
Relevant EMDB volumes: EMD-1886
Expression system: Mesocricetus auratus