› 5gvd

X-ray diffraction
1.62Å resolution

Human TDRD3 DUF1767-OB domains

Released:
DOI: 10.2210/pdb5gvd/pdb
PDB entry 5gvd coloured by chain, front view.
PDB entry 5gvd coloured by chain, side view.
PDB entry 5gvd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of the interaction between Topoisomerase IIIβ and the TDRD3 auxiliary factor.
Goto-Ito S, Yamagata A, Takahashi TS, Sato Y, Fukai S
Sci Rep 7 42123 (2017)
PMID: 28176834

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-190662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tudor domain-containing protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 17.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7E2 (Residues: 1-68; Coverage: 10%)
Gene name: TDRD3
Sequence domains: RMI1, N-terminal OB-fold domain

Ligands and Environments

3 bound ligands:
Ligand PO4 2 x PO4
Ligand EDO 3 x EDO
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P65
Unit cell:
a: 85.669Å b: 85.669Å c: 104.207Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.199
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Born to run: control of transcription elongation by RNA polymerase II.
Chen et al. (2018)
7 more

1 mention without citation

Structural basis of the interaction between Topoisomerase IIIβ and the TDRD3 auxiliary factor.
Goto-Ito et al. (2017)