› 6dc9

X-ray diffraction
3Å resolution

Fab/epitope complex of human chimeric monoclonal antibody h4E6 targeting a phosphorylated tau epitope.

Released:
DOI: 10.2210/pdb6dc9/pdb
Model geometry
Fit model/data
PDB entry 6dc9 coloured by chain, front view.
PDB entry 6dc9 coloured by chain, side view.
PDB entry 6dc9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of monoclonal antibodies targeting C-terminal Ser404 region of phosphorylated tau protein.
Chukwu JE, Congdon EE, Sigurdsson EM, Kong XP
MAbs 11 477-488 (2019)
PMID: 30794086

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-210477 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fab heavy chain Chains: H, I
Molecule details ›
Chains: H, I
Length: 219 amino acids
Theoretical weight: 23.14 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Fab light chain Chains: L, M
Molecule details ›
Chains: L, M
Length: 215 amino acids
Theoretical weight: 23.48 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Microtubule-associated protein tau Chains: P, Q

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand PO4 2 x PO4
1 modified residue:
Ligand SEP 4 x SEP

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P21
Unit cell:
a: 79.212Å b: 65.08Å c: 97.439Å
α: 90° β: 112.11° γ: 90°
R-values:
R R work R free
0.208 0.202 0.26
Expression systems:
  • Homo sapiens
  • Not provided

Quick links

Citations

3 review citations

Treatment of Alzheimer's Disease and Blood-Brain Barrier Drug Delivery.
Pardridge WM. (2020)
2 more

2 mentions without citation

Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.
Pinzi et al. (2023)
1 more