Research workbench
Mouse cereblon thalidomide binding domain, selenomethionine derivative
Analyse Mouse cereblon thalidomide binding domain, selenomethionine derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WX1
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein cereblon
- UniProt
- Q8C7D2
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein cereblon | protein | 108 | 11% helix, 42% strand | Q8C7D2 |
| B | Protein cereblon | protein | 99 | 6% helix, 45% strand | Q8C7D2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 382 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
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 Q8C7D2
- Elsewhere: RCSB PDB 3WX1 · PDBe 3WX1 · UniProt Q8C7D2
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