› 2y1w

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR

Released:
DOI: 10.2210/pdb2y1w/pdb
PDB entry 2y1w coloured by chain, front view.
PDB entry 2y1w coloured by chain, side view.
PDB entry 2y1w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for CARM1 inhibition by indole and pyrazole inhibitors.
Sack JS, Thieffine S, Bandiera T, Fasolini M, Duke GJ, Jayaraman L, Kish KF, Klei HE, Purandare AV, Rosettani P, Troiani S, Xie D, Bertrand JA
Biochem J 436 331-9 (2011)
PMID: 21410432

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183246 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 348 amino acids
Theoretical weight: 39.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86X55 (Residues: 135-482; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SFG 4 x SFG
Ligand 849 4 x 849
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 74.896Å b: 98.471Å c: 207.184Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.244
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Epigenetic protein families: a new frontier for drug discovery.
Arrowsmith et al. (2012)
17 more

10 mentions without citation

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