6dvr

X-ray diffraction
1.54Å resolution

Crystal structure of human CARM1 with (R)-SKI-72

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zeng H, Hutchinson A, Seitova A, Luo M, Cai XC, Ke W, Wang J, Shi C, Zheng W, Lee JP, Ibanez G, Bountra C, Arrowsmith CH, Edwards AM, Brown PJ, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
PDBe Complex ID:
PDB-CPX-183245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-arginine methyltransferase CARM1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.98 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q86X55 (Residues: 146-489; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains: Ribosomal protein L11 methyltransferase (PrmA)
Structure domains: Hnrnp arginine n-methyltransferase1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I222
Unit cell:
a: 74.366Å b: 98.579Å c: 207.375Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.215
Expression system: Spodoptera frugiperda