MolNFT v1 · #393272 · protein
AlphaFold monomer V2.0 prediction for exosome complex component RRP42 (O29756)
O29756: “AlphaFold monomer V2.0 prediction for exosome complex component RRP42 (O29756)”. 1 pocket (best druggability 0.68). MolNFT v1 #393272 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O29756
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Exosome complex component RRP42
- UniProt
- O29756
- Pockets
- 1 · best druggability 0.68
Structure
1 distinct chain · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exosome complex component RRP42 | protein | 259 | 32% helix, 31% strand | O29756 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 307 | 0.68 | 0.83 | 28 | empty |
Compared structures
- 3M85 · Archaeoglobus fulgidus exosome Y70A with RNA bound to the active site · an experimental structure of the same protein · chain A against I, TM-score 0.99
- 3M85 · Archaeoglobus fulgidus exosome y70a with RNA bound to the active site · an experimental structure of the same protein · chain A against I, TM-score 0.99
- 3M7N · Archaeoglobus fulgidus exosome with RNA bound to the active site · an experimental structure of the same protein · chain A against H, TM-score 0.99
- 3M7N · archaeoglobus fulgidus exosome with RNA bound to the active site · an experimental structure of the same protein · chain A against H, TM-score 0.99
- 2BA0 · Archaeal exosome core · an experimental structure of the same protein · chain A against H, TM-score 0.98
- 2BA0 · Archaeal exosome core · an experimental structure of the same protein · chain A against H, TM-score 0.98
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 O29756
- Elsewhere: UniProt O29756 · AlphaFold DB O29756
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