› 7os4

X-ray diffraction
2.54Å resolution

Crystal structure of mouse CARM1 in complex with histone H3_13-31 K18

Released:
DOI: 10.2210/pdb7os4/pdb
PDB entry 7os4 coloured by chain, front view.
PDB entry 7os4 coloured by chain, side view.
PDB entry 7os4 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors.
Zhang Y, Marechal N, van Haren MJ, Troffer-Charlier N, Cura V, Cavarelli J, Martin NI
OpenAccess logo Chembiochem 22 3469-3476 (2021)
PMID: 34569136

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159469 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-arginine methyltransferase CARM1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 371 amino acids
Theoretical weight: 41.99 KDa
Source organism: Mus musculus
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
  • Canonical: Q9WVG6 (Residues: 130-497; Coverage: 61%)
Gene names: Carm1, Prmt4
Sequence domains:
Histone H3.1 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 20 amino acids
Theoretical weight: 1.98 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P68433 (Residues: 14-32; Coverage: 14%)
Gene names: H3.1-221, H3.1-291, H3.1-I, H3a, H3c1, H3c10, H3c11, H3c8, H3g, H3h, H3i, Hist1h3a, Hist1h3g, Hist1h3h, Hist1h3i

Ligands and Environments

1 bound ligand:
Ligand QVR 4 x QVR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-X
Spacegroup: P21212
Unit cell:
a: 74.374Å b: 98.606Å c: 206.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.255
Expression systems:
  • Spodoptera aff. frugiperda 1 BOLD-2017
  • Not provided

Quick links

Citations

1 citations in other articles

A Direct Assay for Measuring the Activity and Inhibition of Coactivator-Associated Arginine Methyltransferase 1.
Zhang et al. (2022)

1 mention without citation

Structural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors.
Zhang et al. (2021)