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Crystal Structure of EED in Complex with UNC4859

Analyse Crystal Structure of EED in Complex with UNC4859 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TTW
Type
protein
Length
728 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.74
Source
Homo sapiens; SYNTHETIC CONSTRUCT
Molecule
Polycomb protein EED; UNC4859
UniProt
O75530
Ligands
UNX, SO4
Pockets
9 · best druggability 0.76

Structure

x-ray diffraction · resolution 1.74 · 3 distinct chains · 5% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolycomb protein EEDprotein3607% helix, 48% strandO75530
B, DUNC4859protein50% helix, 0% strand—
CPolycomb protein EEDprotein3584% helix, 47% strandO75530

Ligands and binding sites

  • UNX · Unknown atom or ion · ion · 22 copies · chains A, C, D
  • SO4 · Sulfate ion · ion · 2 copies · chains A, C

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

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14830.760.8438empty
24380.760.8543empty
3990.750.9621empty
41750.420.7432UNX
51400.410.7527empty

Interfaces

3 interfaces between chains.

  • A–C · 852 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 433 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 430 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (methylation, nonstandard).

Compared structures

  • 5TTW · Crystal structure of eed in complex with UNC4859 · the same entry in another collection · chain A against A, TM-score 1.00
  • O75530 · AlphaFold monomer V2.0 prediction for polycomb protein eed (O75530) · a predicted model of the same protein · chain A against A, TM-score 0.99

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