Research workbench
AlphaFold monomer V2.0 prediction for adenylate-forming reductase NPS11 (F8P9P5)
Analyse AlphaFold monomer V2.0 prediction for adenylate-forming reductase NPS11 (F8P9P5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F8P9P5
- Type
- protein
- Length
- 1,099 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Adenylate-forming reductase NPS11
- UniProt
- F8P9P5
- Pockets
- 12 · best druggability 0.83
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate-forming reductase NPS11 | protein | 1099 | 42% helix, 16% strand | F8P9P5 |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.83 | 0.84 | 103 | empty |
| 2 | 1020 | 0.81 | 0.83 | 113 | empty |
| 3 | 233 | 0.68 | 0.84 | 31 | empty |
| 4 | 180 | 0.58 | 0.81 | 25 | empty |
| 5 | 124 | 0.53 | 0.82 | 24 | 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 F8P9P5
- Elsewhere: UniProt F8P9P5 · AlphaFold DB F8P9P5
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