8shb

X-ray diffraction
2.09Å resolution

Crystal Structure of PRMT3 with Compound YD1-208

Released:
Source organism: Homo sapiens
Entry authors: Song X, Dong A, Deng Y, Huang R, Arrowsmith CH, Edwards AM, Min J, 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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-130068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 3 Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 38.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60678 (Residues: 211-531; Coverage: 61%)
Gene names: HRMT1L3, PRMT3
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P43212
Unit cell:
a: 70.14Å b: 70.14Å c: 172.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.238
Expression system: Escherichia coli