› 5j39

X-ray diffraction
1.95Å resolution

Crystal Structure of the extended TUDOR domain from TDRD2

Released:
DOI: 10.2210/pdb5j39/pdb
PDB entry 5j39 coloured by chain, front view.
PDB entry 5j39 coloured by chain, side view.
PDB entry 5j39 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.
Zhang H, Liu K, Izumi N, Huang H, Ding D, Ni Z, Sidhu SS, Chen C, Tomari Y, Min J
Proc Natl Acad Sci U S A 114 12483-12488 (2017)
PMID: 29118143

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tudor and KH domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y2W6 (Residues: 309-498; Coverage: 34%)
Gene names: TDRD2, TDRKH
Sequence domains: Tudor domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CAC 2 x CAC
Ligand UNX 18 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 36.692Å b: 53.798Å c: 108.063Å
α: 90° β: 84.26° γ: 90°
R-values:
R R work R free
0.192 0.19 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration.
St George-Hyslop et al. (2018)
2 more

1 mention without citation

Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.
Zhang et al. (2017)