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Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with sah

Analyse Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4C05
Type
protein
Length
318 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 6
EC
2.1.1.-, 2.1.1.125
UniProt
Q6NZB1
Ligands
SAH
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 6 (EC 2.1.1.-, 2.1.1.125)protein31828% helix, 37% strandQ6NZB1

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13350.620.7940SAH
2700.560.8817empty

Compared structures

  • 4C05 · Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH · 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 A against A, TM-score 0.99

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