6mw9

Electron Microscopy
7.3Å resolution

CryoEM structure of chimeric Eastern Equine Encephalitis Virus with Fab of EEEV-3 antibody

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:
hetero 960-mer (preferred)
PDBe Complex ID:
PDB-CPX-207871 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Spike glycoprotein E1 Chains: A, E, I, M
Molecule details ›
Chains: A, E, I, M
Length: 441 amino acids
Theoretical weight: 47.94 KDa
Source organism: Eastern equine encephalitis virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: Q4QXJ7 (Residues: 802-1242; Coverage: 36%)
Sequence domains: Alphavirus E1 glycoprotein
Spike glycoprotein E2 Chains: B, F, J, N
Molecule details ›
Chains: B, F, J, N
Length: 420 amino acids
Theoretical weight: 47.05 KDa
Source organism: Eastern equine encephalitis virus
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: Q4QXJ7 (Residues: 325-744; Coverage: 34%)
Sequence domains: Alphavirus E2 glycoprotein
EEEV-3 antibody heavy chain Chains: C, G, K, O
Molecule details ›
Chains: C, G, K, O
Length: 218 amino acids
Theoretical weight: 23.74 KDa
Source organism: Mus musculus
Ig-like domain-containing protein Chains: D, H, L, P
Molecule details ›
Chains: D, H, L, P
Length: 214 amino acids
Theoretical weight: 23.18 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: G0YP42 (Residues: 20-233; Coverage: 100%)
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.3Å
Relevant EMDB volumes: EMD-9274
Expression system: Mesocricetus auratus