Research workbench
AlphaFold monomer V2.0 prediction for stress response protein NST1 (Q2GZN9)
Analyse AlphaFold monomer V2.0 prediction for stress response protein NST1 (Q2GZN9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2GZN9
- Type
- protein
- Length
- 1,255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1476E256abc44781fb156B17e3931B8F4A8c7FAB
- Molecule
- Stress response protein NST1
- UniProt
- Q2GZN9
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 27% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stress response protein NST1 | protein | 1255 | 27% helix, 2% strand | Q2GZN9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.78 | 0.80 | 81 | empty |
| 2 | 290 | 0.67 | 0.83 | 32 | empty |
| 3 | 111 | 0.37 | 0.74 | 14 | empty |
| 4 | 116 | 0.35 | 0.73 | 22 | 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 Q2GZN9
- Elsewhere: UniProt Q2GZN9 · AlphaFold DB Q2GZN9
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