3inu

X-ray diffraction
2.5Å resolution

Crystal structure of an unbound KZ52 neutralizing anti-Ebolavirus antibody.

Released:
Source organism: Homo sapiens
Primary publication:
Techniques and tactics used in determining the structure of the trimeric ebolavirus glycoprotein.
Acta Crystallogr. D Biol. Crystallogr. 65 1162-80 (2009)
PMID: 19923712

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
KZ52 antibody fragment heavy chain Chains: H, M
Molecule details ›
Chains: H, M
Length: 226 amino acids
Theoretical weight: 24.02 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
KZ52 antibody fragment light chain Chains: L, N
Molecule details ›
Chains: L, N
Length: 217 amino acids
Theoretical weight: 23.9 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3221
Unit cell:
a: 129.52Å b: 129.52Å c: 184.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.252
Expression system: Cricetulus griseus