Research workbench
AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa 1 (Q92S10)
Analyse AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92S10
- Type
- protein
- Length
- 503 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Ribose import ATP-binding protein rbsa 1
- UniProt
- Q92S10
- Pockets
- 3 · best druggability 0.62
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose import ATP-binding protein rbsa 1 | protein | 503 | 36% helix, 26% strand | Q92S10 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.62 | 0.76 | 66 | empty |
| 2 | 184 | 0.57 | 0.81 | 24 | empty |
| 3 | 65 | 0.28 | 0.73 | 16 | 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 Q92S10
- Elsewhere: UniProt Q92S10 · AlphaFold DB Q92S10
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