› 6s79

X-ray diffraction
2.1Å resolution

Crystal structure of CARM1 in complex with inhibitor AA183

Released:
DOI: 10.2210/pdb6s79/pdb
Model geometry
Fit model/data
PDB entry 6s79 coloured by chain, front view.
PDB entry 6s79 coloured by chain, side view.
PDB entry 6s79 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).
Gunnell EA, Al-Noori A, Muhsen U, Davies CC, Dowden J, Dreveny I
OpenAccess logo Biochem J 477 787-800 (2020)
PMID: 32011657

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183245 (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: 351 amino acids
Theoretical weight: 40.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86X55 (Residues: 135-479; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand KXW 4 x KXW
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21212
Unit cell:
a: 75.479Å b: 99.196Å c: 208.439Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.231
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A unique binding pocket induced by a noncanonical SAH mimic to develop potent and selective PRMT inhibitors.
Deng et al. (2023)
1 more

2 mentions without citation

A Pan-Inhibitor for Protein Arginine Methyltransferase Family Enzymes.
Iyamu et al. (2021)
1 more