Research workbench
AlphaFold monomer V2.0 prediction for GTP-binding nuclear protein ran (P41915)
Analyse AlphaFold monomer V2.0 prediction for GTP-binding nuclear protein ran (P41915) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P41915
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0944786f8d97650C95AfEbF84205C238dB68d6b1
- Molecule
- GTP-binding nuclear protein ran
- UniProt
- P41915
- Pockets
- 4 · best druggability 0.49
Structure
1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding nuclear protein ran | protein | 225 | 32% helix, 21% strand | P41915 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.49 | 0.80 | 16 | empty |
| 2 | 114 | 0.49 | 0.81 | 28 | empty |
| 3 | 77 | 0.39 | 0.78 | 13 | empty |
| 4 | 54 | 0.30 | 0.76 | 11 | 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 P41915
- Elsewhere: UniProt P41915 · AlphaFold DB P41915
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