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The yth domain of YTHDC1 protein in complex with GM6ACU oligonucleotide

Analyse The yth domain of YTHDC1 protein in complex with GM6ACU oligonucleotide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RT7
Type
protein + RNA
Length
327 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Yth domain-containing protein 1; RNA (5'-R(*(6MZ)P*C)-3')
UniProt
Q96MU7
Ligands
6MZ, SO4
Pockets
6 · best druggability 0.49

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BYth domain-containing protein 1protein16033% helix, 26% strandQ96MU7
CYth domain-containing protein 1protein16431% helix, 26% strandQ96MU7
ERNA (5'-R(*(6MZ)P*C)-3')rna3——

Ligands and binding sites

  • 6MZ · N6-methyladenosine-5'-monophosphate · ligand · chains C
  • SO4 · Sulfate ion · ion · 5 copies · chains B, C

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

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.490.83166MZ
2690.430.8117empty
3930.420.7816empty
4980.410.7716empty
5890.320.7318empty

Interfaces

2 interfaces between chains.

  • B–E · 612 Ų buried · 17 hydrogen bonds · protein-nucleic
  • B–C · 238 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nucleotide modification).

Compared structures

  • 6RT7 · The YTH domain of YTHDC1 protein in complex with Gm6ACU oligonucleotide · the same entry in another collection · chain B against B, TM-score 1.00
  • Q96MU7 · AlphaFold monomer V2.0 prediction for yth domain-containing protein 1 (Q96MU7) · a predicted model of the same protein · chain C against A, TM-score 0.98

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