› 5llk

X-ray diffraction
1.8Å resolution

Crystal structure of human alpha-dystroglycan

Released:
DOI: 10.2210/pdb5llk/pdb
PDB entry 5llk coloured by chain, front view.
PDB entry 5llk coloured by chain, side view.
PDB entry 5llk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural flexibility of human α-dystroglycan.
Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A
FEBS Open Bio 7 1064-1077 (2017)
PMID: 28781947

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171921 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-dystroglycan Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14118 (Residues: 52-315; Coverage: 31%)
Gene name: DAG1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R3
Unit cell:
a: 71.52Å b: 71.52Å c: 144.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.195
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

A molecular overview of the primary dystroglycanopathies.
Brancaccio A. (2019)
2 more

2 mentions without citation

Target specificity of selective bioactive compounds in blocking α-dystroglycan receptor to suppress Lassa virus infection: an in silico approach.
Arefin et al. (2021)
1 more