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Crystal structure of M. musculus protein arginine methyltransferase PRMT6 reduced

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

PDB
4C03
Type
protein
Length
665 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.-, 2.1.1.125
UniProt
Q6NZB1
Ligands
SFG
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 6 (EC 2.1.1.-, 2.1.1.125)protein33733% helix, 35% strandQ6NZB1
BProtein arginine N-methyltransferase 6 (EC 2.1.1.-, 2.1.1.125)protein32830% helix, 38% strandQ6NZB1

Ligands and binding sites

  • SFG · Sinefungin · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12120.740.8939SFG
22770.730.8644SFG
31190.510.8121empty
41100.510.8126empty
5580.290.7413empty

Interfaces

1 interface between chains.

  • A–B · 1755 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 4C03 · Crystal structure of M. musculus protein arginine methyltransferase PRMT6 reduced · 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 1.00

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