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8g2g

X-ray diffraction
2.02Å resolution

Crystal structure of PRMT3 with compound YD1113

Released:
Model geometry
Fit model/data

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(+)., L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+).]
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 Chains: A, B
Molecule details ›
Chains: A, B
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

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2221
Unit cell:
a: 95.808Å b: 99.863Å c: 170.314Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.232
Expression system: Escherichia coli