› 4hsi

X-ray diffraction
3.1Å resolution

Glycoprotein B from Herpes simplex virus type 1, A504P/R505G/Q507G/N511G mutant, low-pH

Released:
DOI: 10.2210/pdb4hsi/pdb
PDB entry 4hsi coloured by chain, front view.
PDB entry 4hsi coloured by chain, side view.
PDB entry 4hsi coloured by chain, top view.
Source organism: Human alphaherpesvirus 1 strain KOS
Primary publication:
Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form.
Vitu E, Sharma S, Stampfer SD, Heldwein EE
J Mol Biol 425 2056-2071 (2013)
PMID: 23500487

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Envelope glycoprotein B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 703 amino acids
Theoretical weight: 78.7 KDa
Source organism: Human alphaherpesvirus 1 strain KOS
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P06437 (Residues: 61-730; Coverage: 77%)
Gene names: UL27, gB
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 6 x NAG
Ligand MRY 2 x MRY
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3
Unit cell:
a: 117.295Å b: 117.295Å c: 321.872Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.205 0.255
Expression system: Spodoptera frugiperda

Quick links

Citations

6 review citations

Virus and cell fusion mechanisms.
Podbilewicz B. (2014)
5 more

2 mentions without citation

Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form.
Vitu et al. (2013)
1 more