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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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polycomb protein EED | protein | 360 | 7% helix, 48% strand | O75530 |
| B, D | UNC4859 | protein | 5 | 0% helix, 0% strand | — |
| C | Polycomb protein EED | protein | 358 | 4% helix, 47% strand | O75530 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 483 | 0.76 | 0.84 | 38 | empty |
| 2 | 438 | 0.76 | 0.85 | 43 | empty |
| 3 | 99 | 0.75 | 0.96 | 21 | empty |
| 4 | 175 | 0.42 | 0.74 | 32 | UNX |
| 5 | 140 | 0.41 | 0.75 | 27 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O75530
- Elsewhere: RCSB PDB 5TTW · PDBe 5TTW · UniProt O75530
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