PDBe 3csy

X-ray diffraction
3.4Å resolution

Crystal structure of the trimeric prefusion Ebola virus glycoprotein in complex with a neutralizing antibody from a human survivor

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Fab KZ52 heavy chain Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 226 amino acids
Theoretical weight: 24.21 KDa
Structure domains: Immunoglobulins
Fab KZ52 light chain Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 217 amino acids
Theoretical weight: 23.94 KDa
Structure domains: Immunoglobulins
GP1 Chains: I, K, M, O
Molecule details ›
Chains: I, K, M, O
Length: 334 amino acids
Theoretical weight: 37.03 KDa
Source organism: Ebola virus - Mayinga, Zaire, 1976
Expression system: Homo sapiens
UniProt:
  • Canonical: Q05320 (Residues: 32-336; Coverage: 47%)
Gene name: GP
GP2 Chains: J, L, N, P
Molecule details ›
Chains: J, L, N, P
Length: 131 amino acids
Theoretical weight: 14.78 KDa
Source organism: Ebola virus - Mayinga, Zaire, 1976
Expression system: Homo sapiens
UniProt:
  • Canonical: Q05320 (Residues: 502-632; Coverage: 20%)
Gene name: GP

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: R32
Unit cell:
a: 273.71Å b: 273.71Å c: 409.43Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 0.261 0.302
Expression system: Homo sapiens