› 6ncq

X-ray diffraction
1.9Å resolution

The dimerization domain of human SFPQ in space group C2221

Released:
DOI: 10.2210/pdb6ncq/pdb
PDB entry 6ncq coloured by chain, front view.
PDB entry 6ncq coloured by chain, side view.
PDB entry 6ncq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.
Hewage TW, Caria S, Lee M
Acta Crystallogr F Struct Biol Commun 75 439-449 (2019)
PMID: 31204691

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149903 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Splicing factor, proline- and glutamine-rich Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 30.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23246 (Residues: 276-535; Coverage: 37%)
Gene names: PSF, SFPQ
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2221
Unit cell:
a: 65.131Å b: 119.167Å c: 72.773Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.243
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Binding and transport of SFPQ-RNA granules by KIF5A/KLC1 motors promotes axon survival.
Fukuda et al. (2021)
3 more

3 mentions without citation

The Emerging Role of the RNA-Binding Protein SFPQ in Neuronal Function and Neurodegeneration.
Lim et al. (2020)
2 more