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Acetyltransferase domain of CDY1

Analyse Acetyltransferase domain of CDY1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FBM
Type
protein
Length
751 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Y chromosome chromodomain protein 1, telomeric isoform B
UniProt
Q9Y6F8
Ligands
CL
Pockets
5 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AY chromosome chromodomain protein 1, telomeric isoform Bprotein25152% helix, 16% strandQ9Y6F8
B, CY chromosome chromodomain protein 1, telomeric isoform Bprotein25054% helix, 16% strandQ9Y6F8

Ligands and binding sites

  • CL · Chloride ion · ion · 3 copies · chains A, 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
15450.830.8971empty
21040.420.7716empty
3940.390.7616empty
4770.390.7815empty
5840.370.7621empty

Interfaces

3 interfaces between chains.

  • A–C · 1234 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1195 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 1164 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 2FBM · Acetyltransferase domain of CDY1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y6F8 · AlphaFold monomer V2.0 prediction for testis-specific chromodomain protein Y 1 (Q9Y6F8) · a predicted model of the same protein · chain A against A, TM-score 1.00

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