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Crystal structure of mus musculus protein arginine methyltransferase 2 with sah

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

PDB
5FUL
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
SAH, CA, CL
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 2 (EC 2.1.1.125)protein33928% helix, 36% strandQ3UKX1

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • CA · Calcium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 2 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14030.740.8450SAH, CA, EDO
2520.270.7416CL

Compared structures

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

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