› 4glr

X-ray diffraction
1.9Å 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-210466 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Microtubule-associated protein tau Chains: A, B
Molecule details ›
Chains: A, B
Length: 18 amino acids
Theoretical weight: 2.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10636 (Residues: 541-557; Coverage: 2%)
Gene names: MAPT, MAPTL, MTBT1, TAU
anti-ptau heavy chain Chains: H, J
Molecule details ›
Chains: H, J
Length: 229 amino acids
Theoretical weight: 23.61 KDa
Source organism: Gallus gallus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
anti-ptau light chain Chains: I, K
Molecule details ›
Chains: I, K
Length: 212 amino acids
Theoretical weight: 22.18 KDa
Source organism: Gallus gallus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
2 modified residues:
Ligand TPO 2 x TPO
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21212
Unit cell:
a: 68.5Å b: 216.5Å c: 70Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.208
Expression systems:
  • Not provided
  • Cricetulus griseus

Quick links

Citations

10 review citations

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
9 more

13 mentions without citation

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