› 5el3

X-ray diffraction
1.59Å resolution

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-131005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
KH domain-containing, RNA-binding, signal transduction-associated protein 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 113 amino acids
Theoretical weight: 13.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75525 (Residues: 50-160; Coverage: 32%)
Gene names: KHDRBS3, SALP, SLM2

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 57.12Å b: 85.92Å c: 59.07Å
α: 90° β: 117.23° γ: 90°
R-values:
R R work R free
0.178 0.176 0.205
Expression system: Escherichia coli

Quick links

Citations

9 review citations

RNA splicing and splicing regulator changes in prostate cancer pathology.
Munkley et al. (2017)
8 more

2 mentions without citation

Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.
Feracci et al. (2016)
1 more