Research workbench
AlphaFold monomer V2.0 prediction for ran-binding protein 17 (Q99NF8)
Analyse AlphaFold monomer V2.0 prediction for ran-binding protein 17 (Q99NF8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99NF8
- Type
- protein
- Length
- 1,088 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7fEd737f2882f99c9830CDF6E0f686eAaa2C02E2
- Molecule
- Ran-binding protein 17
- UniProt
- Q99NF8
- Pockets
- 16 · best druggability 0.69
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ran-binding protein 17 | protein | 1088 | 74% helix, 0% strand | Q99NF8 |
Pockets
16 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 726 | 0.69 | 0.77 | 67 | empty |
| 2 | 295 | 0.54 | 0.75 | 33 | empty |
| 3 | 52 | 0.47 | 0.85 | 14 | empty |
| 4 | 88 | 0.47 | 0.81 | 16 | empty |
| 5 | 116 | 0.43 | 0.77 | 20 | 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 Q99NF8
- Elsewhere: UniProt Q99NF8 · AlphaFold DB Q99NF8
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