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Crystal structure of mus musculus protein arginine methyltransferase 2 with CP1

Analyse Crystal structure of mus musculus protein arginine methyltransferase 2 with CP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5FWA
Type
protein
Length
339 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 2
EC
2.1.1.125
UniProt
Q3UKX1
Ligands
J7C, CA, CL
Pockets
1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 2 (EC 2.1.1.125)protein33927% helix, 36% strandQ3UKX1

Ligands and binding sites

  • J7C · 9-(6-carbamimidamido-5,6-dideoxy-beta-D-ribo-hexofuranosyl)-9H-purin-6-amine · ligand · chains A
  • CA · Calcium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A
  • PG4 · Tetraethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13550.740.8546J7C, EDO

Compared structures

  • 5FWA · Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with CP1 · the same entry in another collection · chain A against A, TM-score 1.00

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