› 2x6m

X-ray diffraction
1.62Å resolution

Structure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein

Released:
DOI: 10.2210/pdb2x6m/pdb
PDB entry 2x6m coloured by chain, front view.
PDB entry 2x6m coloured by chain, side view.
PDB entry 2x6m coloured by chain, top view.
Source organisms:
Primary publication:
Structure and properties of a complex of α-synuclein and a single-domain camelid antibody.
De Genst EJ, Guilliams T, Wellens J, O'Day EM, Waudby CA, Meehan S, Dumoulin M, Hsu ST, Cremades N, Verschueren KH, Pardon E, Wyns L, Steyaert J, Christodoulou J, Dobson CM
J Mol Biol 402 326-43 (2010)
PMID: 20620148

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-211187 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
HEAVY CHAIN VARIABLE DOMAIN FROM DROMEDARY Chain: A
Molecule details ›
Chain: A
Length: 126 amino acids
Theoretical weight: 13.44 KDa
Source organism: Camelus dromedarius
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Alpha-synuclein Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.07 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P37840 (Residues: 132-140; Coverage: 6%)
Gene names: NACP, PARK1, SNCA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 60.17Å b: 63.12Å c: 62.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.156 0.203
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

29 review citations

Nanobodies: natural single-domain antibodies.
Muyldermans S. (2013)
28 more

14 mentions without citation

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)
13 more