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The yth domain of YTHDC1 protein in complex with GGM6AC oligonucleotide

Analyse The yth domain of YTHDC1 protein in complex with GGM6AC oligonucleotide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RT6
Type
protein + RNA
Length
326 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
5 · best druggability 0.51

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 1protein16432% helix, 26% strandQ96MU7
ERNA (5'-R(*(6MZ)P*C)-3')rna2——

Ligands and binding sites

  • 6MZ · N6-methyladenosine-5'-monophosphate · ligand · chains C
  • SO4 · Sulfate ion · ion · 4 copies · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.510.81196MZ
2820.460.8118empty
31150.440.7715empty
41000.420.7716empty
5700.280.7215empty

Interfaces

2 interfaces between chains.

  • B–E · 402 Ų buried · 11 hydrogen bonds · protein-nucleic
  • B–C · 233 Ų buried · 1 hydrogen bond · protein-protein

Modifications

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

Compared structures

  • 6RT6 · The YTH domain of YTHDC1 protein in complex with GGm6AC 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 0.99

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