6ckc

X-ray diffraction
2.8Å resolution

Structure of PRMT5:MEP50 in complex with LLY-283, a potent and selective inhibitor of PRMT5, with antitumor activity

Released:

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:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein arginine N-methyltransferase 5 Chain: A
Molecule details ›
Chain: A
Length: 650 amino acids
Theoretical weight: 74.28 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O14744 (Residues: 1-637; Coverage: 100%)
Gene names: HRMT1L5, IBP72, JBP1, PRMT5, SKB1
Sequence domains:
Methylosome protein 50 Chain: B
Molecule details ›
Chain: B
Length: 344 amino acids
Theoretical weight: 36.88 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9BQA1 (Residues: 2-342; Coverage: 100%)
Gene names: HKMT1069, MEP50, Nbla10071, WD45, WDR77
Sequence domains: WD domain, G-beta repeat

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I222
Unit cell:
a: 102.785Å b: 139.077Å c: 178.961Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Spodoptera frugiperda