Research workbench
AlphaFold monomer V2.0 prediction for nodulation protein noll (P55431)
Analyse AlphaFold monomer V2.0 prediction for nodulation protein noll (P55431) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P55431
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4B90C51942be0dE1D7B37C1DcDfC4fEd2eCF2c32
- Molecule
- Nodulation protein noll
- UniProt
- P55431
- Pockets
- 6 · best druggability 0.71
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nodulation protein noll | protein | 366 | 75% helix, 0% strand | P55431 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 567 | 0.71 | 0.80 | 55 | empty |
| 2 | 477 | 0.67 | 0.78 | 31 | empty |
| 3 | 235 | 0.54 | 0.77 | 29 | empty |
| 4 | 116 | 0.38 | 0.74 | 18 | empty |
| 5 | 106 | 0.38 | 0.74 | 17 | 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 P55431
- Elsewhere: UniProt P55431 · AlphaFold DB P55431
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