› 4mmr

X-ray diffraction
3.1Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136974 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fusion glycoprotein F2 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.22 KDa
Source organism: Human respiratory syncytial virus A2
Expression system: Homo sapiens
UniProt:
  • Canonical: P03420 (Residues: 26-107; Coverage: 15%)
Gene name: F
Fibritin; Fusion glycoprotein F1 Chain: B
Molecule details ›
Chain: B
Length: 414 amino acids
Theoretical weight: 45.58 KDa
Source organisms: Expression system: Homo sapiens
UniProt:
  • Canonical: P03420 (Residues: 137-513; Coverage: 69%)
  • Canonical: P10104 (Residues: 458-484; Coverage: 6%)
Gene names: F, wac
Sequence domains: Fusion glycoprotein F0

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P4132
Unit cell:
a: 170.852Å b: 170.852Å c: 170.852Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.264
Expression system: Homo sapiens

Quick links

Citations

160 review citations

Maternal antibodies: clinical significance, mechanism of interference with immune responses, and possible vaccination strategies.
Niewiesk S. (2014)
159 more

1 mention without citation

A highly stable prefusion RSV F vaccine derived from structural analysis of the fusion mechanism.
Krarup et al. (2015)