Research workbench
AlphaFold monomer V2.0 prediction for protein NDRG1 (Q66IG4)
Analyse AlphaFold monomer V2.0 prediction for protein NDRG1 (Q66IG4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q66IG4
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Protein NDRG1
- UniProt
- Q66IG4
- Pockets
- 5 · best druggability 0.53
Structure
1 distinct chain · 31% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein NDRG1 | protein | 395 | 31% helix, 14% strand | Q66IG4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.53 | 0.77 | 28 | empty |
| 2 | 150 | 0.50 | 0.78 | 17 | empty |
| 3 | 156 | 0.47 | 0.77 | 24 | empty |
| 4 | 116 | 0.44 | 0.78 | 21 | empty |
| 5 | 107 | 0.36 | 0.74 | 16 | empty |
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 Q66IG4
- Elsewhere: UniProt Q66IG4 · AlphaFold DB Q66IG4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.