1x2p

Solution NMR

Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2

Released:
Source organism: Homo sapiens
Entry authors: Chikayama E, Kigawa T, Saito K, Koshiba S, Inoue M, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-157300 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase 2 Chain: A
Molecule details ›
Chain: A
Length: 68 amino acids
Theoretical weight: 7.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P55345 (Residues: 33-87; Coverage: 13%)
Gene names: HMT1, HRMT1L1, PRMT2
Sequence domains: SH3 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics, restrainted molecular dynamics
Expression system: Not provided