Function and Biology Details
Biochemical function:
- not assigned
Biological process:
Cellular component:
- not assigned
Sequence domain:
Structure domain:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Fusion glycoprotein F1 (preferred)
PDBe Complex ID:
PDB-CPX-145706 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fusion glycoprotein F1
Molecule details ›
Chains: A, C, E, G, I, K, M, O, Q, S, U, W
Length: 52 amino acids
Theoretical weight: 5.65 KDa
Source organism: Human respiratory syncytial virus strain RSS-2
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 52 amino acids
Theoretical weight: 5.65 KDa
Source organism: Human respiratory syncytial virus strain RSS-2
Expression system: Escherichia coli
UniProt:
- Canonical:
P11209 (Residues: 158-209; Coverage: 10%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fusion glycoprotein F1
Molecule details ›
Chains: B, D, F, H, J, L, N, P, R, T, V, X
Length: 43 amino acids
Theoretical weight: 4.87 KDa
Source organism: Human respiratory syncytial virus strain RSS-2
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 43 amino acids
Theoretical weight: 4.87 KDa
Source organism: Human respiratory syncytial virus strain RSS-2
Expression system: Escherichia coli
UniProt:
- Canonical: P11209 (Residues: 477-519; Coverage: 8%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSLS BEAMLINE X4A
Spacegroup:
P1
Expression system: Escherichia coli
