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Crystal structure of mouse PRMT6 in complex with inhibitor U2

Analyse Crystal structure of mouse PRMT6 in complex with inhibitor U2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SQ4
Type
protein
Length
661 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 6
EC
2.1.1.319
UniProt
Q6NZB1
Ligands
GJV, IOD
Pockets
3 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 6 (EC 2.1.1.319)protein33631% helix, 37% strandQ6NZB1
BProtein arginine N-methyltransferase 6 (EC 2.1.1.319)protein32530% helix, 37% strandQ6NZB1

Ligands and binding sites

  • GJV · 9-(7-{[amino(iminio)methyl]amino}-5,6,7-trideoxy-beta-D-ribo-heptofuranosyl)-9H-purin-6-amine · ligand · 2 copies · chains A, B
  • IOD · Iodide ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12250.790.9240GJV
25190.730.8260GJV
3940.460.8021empty

Interfaces

1 interface between chains.

  • A–B · 1819 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6SQ4 · Crystal structure of mouse PRMT6 in complex with inhibitor U2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6NZB1 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q6NZB1) · a predicted model of the same protein · chain B against A, TM-score 0.99

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