› 5csz

X-ray diffraction
1.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209166 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
GANTENERUMAB FAB FRAGMENT HEAVY CHAIN Chains: A, H
Molecule details ›
Chains: A, H
Length: 228 amino acids
Theoretical weight: 24.21 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
GANTENERUMAB FAB FRAGMENT LIGHT CHAIN Chains: B, L
Molecule details ›
Chains: B, L
Length: 215 amino acids
Theoretical weight: 23.36 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
Amyloid-beta protein 40 Chains: D, E
Molecule details ›
Chains: D, E
Length: 11 amino acids
Theoretical weight: 1.33 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-682; Coverage: 2%)
Gene names: A4, AD1, APP

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 71.137Å b: 66.242Å c: 105.156Å
α: 90° β: 99.09° γ: 90°
R-values:
R R work R free
0.198 0.196 0.23
Expression systems:
  • Cricetulus griseus
  • Not provided

Quick links

Citations

97 review citations

Tau aggregation and its interplay with amyloid-β.
Nisbet et al. (2015)
96 more

6 mentions without citation

Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes.
Ma et al. (2016)
5 more