› 5e8r

X-ray diffraction
2.55Å resolution

Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae)

Released:
DOI: 10.2210/pdb5e8r/pdb
PDB entry 5e8r coloured by chain, front view.
PDB entry 5e8r coloured by chain, side view.
PDB entry 5e8r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases.
Eram MS, Shen Y, Szewczyk M, Wu H, Senisterra G, Li F, Butler KV, Kaniskan HÜ, Speed BA, Dela Seña C, Dong A, Zeng H, Schapira M, Brown PJ, Arrowsmith CH, Barsyte-Lovejoy D, Liu J, Vedadi M, Jin J
ACS Chem Biol 11 772-781 (2016)
PMID: 26598975

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 376 amino acids
Theoretical weight: 42.07 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q96LA8 (Residues: 1-375; Coverage: 100%)
Gene names: HRMT1L6, PRMT6
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SAH 2 x SAH
Ligand 5L6 2 x 5L6
Ligand CL 5 x CL
Ligand UNX 9 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P43
Unit cell:
a: 100.244Å b: 100.244Å c: 89.868Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.22 0.256
Expression system: Spodoptera frugiperda

Quick links

Citations

35 review citations

Arginine Methylation: The Coming of Age.
Blanc et al. (2017)
34 more

9 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
8 more