Research workbench
AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa (Q4QN44)
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
- Q4QN44
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBABc9DC7023be831DDdB1D7F196c6336E7D131B7
- Molecule
- Ribose import ATP-binding protein rbsa
- UniProt
- Q4QN44
- Pockets
- 6 · best druggability 0.50
Structure
1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose import ATP-binding protein rbsa | protein | 493 | 37% helix, 28% strand | Q4QN44 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.50 | 0.76 | 29 | empty |
| 2 | 106 | 0.46 | 0.79 | 18 | empty |
| 3 | 169 | 0.45 | 0.75 | 26 | empty |
| 4 | 86 | 0.38 | 0.77 | 15 | empty |
| 5 | 79 | 0.32 | 0.74 | 15 | 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 Q4QN44
- Elsewhere: UniProt Q4QN44 · AlphaFold DB Q4QN44
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