Research workbench
AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa (Q5KUX3)
Analyse AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5KUX3
- Type
- protein
- Length
- 494 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- Ribose import ATP-binding protein rbsa
- UniProt
- Q5KUX3
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose import ATP-binding protein rbsa | protein | 494 | 36% helix, 27% strand | Q5KUX3 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 635 | 0.65 | 0.75 | 85 | empty |
| 2 | 53 | 0.61 | 0.93 | 22 | empty |
| 3 | 171 | 0.54 | 0.79 | 19 | empty |
| 4 | 99 | 0.35 | 0.73 | 21 | empty |
| 5 | 68 | 0.30 | 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 Q5KUX3
- Elsewhere: UniProt Q5KUX3 · AlphaFold DB Q5KUX3
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