› 4a4g

Solution NMR

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

Released:
DOI: 10.2210/pdb4a4g/pdb
PDB entry 4a4g coloured by chain, ensemble of 20 models, front view.
PDB entry 4a4g coloured by chain, ensemble of 20 models, side view.
PDB entry 4a4g coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins.
Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, Fischer U, Neugebauer KM, Sattler M
Nat Struct Mol Biol 18 1414-20 (2011)
PMID: 22101937

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Survival motor neuron protein Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16637 (Residues: 84-147; Coverage: 22%)
Gene names: SMN, SMN1, SMN2, SMNC, SMNT
Sequence domains: Survival motor neuron protein (SMN), Tudor domain
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
Ligand DA2 1 x DA2
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

36 review citations

Protein arginine methyltransferases and cancer.
Yang et al. (2013)
35 more

3 mentions without citation

Chemical biology of protein arginine modifications in epigenetic regulation.
Fuhrmann et al. (2015)
2 more