› 6eho

X-ray diffraction
3.5Å resolution

Dimer of the Sortilin Vps10p domain at low pH

Released:
DOI: 10.2210/pdb6eho/pdb
PDB entry 6eho coloured by chain, front view.
PDB entry 6eho coloured by chain, side view.
PDB entry 6eho coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acidic Environment Induces Dimerization and Ligand Binding Site Collapse in the Vps10p Domain of Sortilin.
Januliene D, Andersen JL, Nielsen JA, Quistgaard EM, Hansen M, Strandbygaard D, Moeller A, Petersen CM, Madsen P, Thirup SS
Structure 25 1809-1819.e3 (2017)
PMID: 29107483

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189213 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Sortilin Chain: A
Molecule details ›
Chain: A
Length: 723 amino acids
Theoretical weight: 80.38 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: Q99523 (Residues: 34-756; Coverage: 91%)
Gene name: SORT1
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I213
Unit cell:
a: 189.01Å b: 189.01Å c: 189.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.272
Expression system: Cricetulus griseus

Quick links

Citations

3 review citations

Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors.
Chataigner et al. (2020)
2 more

1 mention without citation

An Allosteric Binding Site on Sortilin Regulates the Trafficking of VLDL, PCSK9, and LDLR in Hepatocytes.
Sparks et al. (2020)