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Crystal structure of mouse PRMT6 with modified H7-4 peptide

Analyse Crystal structure of mouse PRMT6 with modified H7-4 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SQK
Type
protein
Length
679 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein arginine N-methyltransferase 6; H4-7
EC
2.1.1.319, 2.1.1.43
UniProt
Q6NZB1
Pockets
6 · best druggability 0.55

Structure

x-ray diffraction · 4 distinct chains · 31% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein arginine N-methyltransferase 6 (EC 2.1.1.319)protein33731% helix, 35% strandQ6NZB1
BProtein arginine N-methyltransferase 6 (EC 2.1.1.319)protein33331% helix, 37% strandQ6NZB1
DH4-7 (EC 2.1.1.43)protein30% helix, 0% strand—
EH4-7 (EC 2.1.1.43)protein60% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11470.550.8229empty
21070.510.8228empty
31000.390.7615empty
41010.360.7413empty
5540.260.7414empty

Interfaces

3 interfaces between chains.

  • A–B · 1768 Ų buried · 16 hydrogen bonds · protein-protein
  • A–E · 738 Ų buried · 22 hydrogen bonds · protein-protein
  • B–D · 581 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

  • 6SQK · Crystal structure of mouse PRMT6 with modified H7-4 peptide · 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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