› 4fed

X-ray diffraction
2.81Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142540 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Huntingtin; Maltose/maltodextrin-binding periplasmic protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 452 amino acids
Theoretical weight: 50.11 KDa
Source organisms: Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AEX9 (Residues: 27-384; Coverage: 97%)
  • Canonical: P42858 (Residues: 1-17, 18-64; Coverage: 2%)
Gene names: HD, HTT, IT15, JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand ZN 35 x ZN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 153.182Å b: 177.357Å c: 78.346Å
α: 90° β: 108.67° γ: 90°
R-values:
R R work R free
0.239 0.237 0.269
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Huntington disease: natural history, biomarkers and prospects for therapeutics.
Ross et al. (2014)
6 more

3 mentions without citation

Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues.
Kim M. (2013)
2 more