4a4h

Solution NMR

Solution structure of SPF30 Tudor domain in complex with asymmetrically dimethylated arginine

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Survival of motor neuron-related-splicing factor 30 Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 6.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75940 (Residues: 65-128; Coverage: 27%)
Gene names: SMNDC1, SMNR, SPF30
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing
Chemical shifts: BMR18008  
Expression system: Escherichia coli