X-ray diffraction
2.45Å resolution

Crystal Structure of Human Protein arginine N-methyltransferase 6 (PRMT6) in complex with MT2739 inhibitor

Source organism: Homo sapiens
Entry authors: Halabelian L, Zeng H, Dong A, Schapira M, De Freitas RF, Hutchinson A, Seitova A, Bountra C, Edwards AM, Arrowsmith CH, 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
Biochemical function:
Cellular component:

Structure analysis Details

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

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I41
Unit cell:
a: 94.068Å b: 94.068Å c: 109.242Å
α: 90° β: 90° γ: 90°
R R work R free
0.194 0.193 0.226
Expression system: Spodoptera frugiperda