› 3mcl

X-ray diffraction
1.7Å resolution

Anti-beta-amyloid antibody c706 fab in space group P21

Released:
DOI: 10.2210/pdb3mcl/pdb
PDB entry 3mcl coloured by chain, front view.
PDB entry 3mcl coloured by chain, side view.
PDB entry 3mcl coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
His-tag binding by antibody C706 mimics β-amyloid recognition.
Teplyakov A, Obmolova G, Canziani G, Zhao Y, Gutshall L, Jung SS, Gilliland GL
J Mol Recognit 24 570-5 (2011)
PMID: 20842634

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208626 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
C706 MONOCLONAL LIGHT CHAIN Chain: L
Molecule details ›
Chain: L
Length: 212 amino acids
Theoretical weight: 23.07 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Immunoglobulin heavy constant gamma 1 Chain: H
Molecule details ›
Chain: H
Length: 228 amino acids
Theoretical weight: 24.2 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P01857 (Residues: 1-107; Coverage: 27%)
Gene name: IGHG1
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 47.33Å b: 62.79Å c: 68.6Å
α: 90° β: 95.06° γ: 90°
R-values:
R R work R free
0.205 0.203 0.26
Expression system: Homo sapiens

Quick links

Citations

2 citation in other articles

Design of nonapeptide LVFFARKHH: A bifunctional agent against Cu2+ -mediated amyloid β-protein aggregation and cytotoxicity.
Zhang et al. (2018)
1 more

5 mentions without citation

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