3j0f

Electron Microscopy
7Å resolution

Sindbis virion

Released:
Source organism: Sindbis virus
Related structures: EMD-5251

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

Assemblies composition:
hetero 720-mer (preferred)
hetero dodecamer
hetero 60-mer
hetero 72-mer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Capsid protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 29.41 KDa
Source organism: Sindbis virus
UniProt:
  • Canonical: P03316 (Residues: 1-264; Coverage: 21%)
Spike glycoprotein E1 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 439 amino acids
Theoretical weight: 47.42 KDa
Source organism: Sindbis virus
UniProt:
  • Canonical: P03316 (Residues: 807-1245; Coverage: 35%)
Spike glycoprotein E2 Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 423 amino acids
Theoretical weight: 46.98 KDa
Source organism: Sindbis virus
UniProt:
  • Canonical: P03316 (Residues: 329-751; 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-5251