2lto

Solution NMR

TDRD3 complex

Released:
Source organism: Homo sapiens
Primary publication:
Recognition of asymmetrically dimethylated arginine by TDRD3.
Nucleic Acids Res 40 11748-55 (2012)
PMID: 23066109

Function and Biology Details

Reaction catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-150307 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tudor domain-containing protein 3 Chain: A
Molecule details ›
Chain: A
Length: 58 amino acids
Theoretical weight: 6.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7E2 (Residues: 554-608; Coverage: 8%)
Gene name: TDRD3
Sequence domains: Tudor domain
Structure domains: SH3 type barrels.
DNA-directed RNA polymerase II subunit RPB1 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P24928 (Residues: 1804-1816; Coverage: 1%)
Gene names: POLR2, POLR2A
Sequence domains: RNA polymerase Rpb1 C-terminal repeat

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided