› 5dx1

X-ray diffraction
1.93Å resolution

Crystal structure of CARM1, sinefungin, and PABP1 peptide (R455)

Released:
DOI: 10.2210/pdb5dx1/pdb
Model geometry
Fit model/data
PDB entry 5dx1 coloured by chain, front view.
PDB entry 5dx1 coloured by chain, side view.
PDB entry 5dx1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
Boriack-Sjodin PA, Jin L, Jacques SL, Drew A, Sneeringer C, Scott MP, Moyer MP, Ribich S, Moradei O, Copeland RA
ACS Chem Biol 11 763-71 (2016)
PMID: 26551522

Function and Biology Details

Reaction catalysed: 
L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146004 (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: 349 amino acids
Theoretical weight: 39.62 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q86X55 (Residues: 134-479; Coverage: 57%)
Gene names: CARM1, PRMT4
Sequence domains:
Structure domains:
Polyadenylate-binding protein 1 Chains: F, G, H, I
Molecule details ›
Chains: F, G, H, I
Length: 19 amino acids
Theoretical weight: 1.92 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11940 (Residues: 449-466; Coverage: 3%)
Gene names: PAB1, PABP, PABP1, PABPC1, PABPC2

Ligands and Environments

2 bound ligands:
Ligand SFG 4 x SFG
Ligand GOL 4 x GOL
1 modified residue:
Ligand NMM 4 x NMM

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 75.002Å b: 98.322Å c: 208.152Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.238
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

6 review citations

Protein arginine methylation: from enigmatic functions to therapeutic targeting.
Wu et al. (2021)
5 more

3 mentions without citation

Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1.
van Haren et al. (2017)
2 more