Research workbench
AlphaFold monomer V2.0 prediction for stress response protein NST1 (Q0CP15)
Analyse AlphaFold monomer V2.0 prediction for stress response protein NST1 (Q0CP15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0CP15
- Type
- protein
- Length
- 1,129 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x045a1b77c52d845d6e7Ba6a444600C064C71354A
- Molecule
- Stress response protein NST1
- UniProt
- Q0CP15
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 33% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stress response protein NST1 | protein | 1129 | 33% helix, 1% strand | Q0CP15 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 728 | 0.74 | 0.79 | 64 | empty |
| 2 | 159 | 0.45 | 0.75 | 19 | empty |
| 3 | 54 | 0.29 | 0.75 | 10 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q0CP15
- Elsewhere: UniProt Q0CP15 · AlphaFold DB Q0CP15
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