Research workbench
AlphaFold monomer V2.0 prediction for ribose import ATP-binding protein rbsa (Q11C01)
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
- Q11C01
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa5bBccF395a3ABe9B629B9f9f8fBd173cC6F75b8
- Molecule
- Ribose import ATP-binding protein rbsa
- UniProt
- Q11C01
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose import ATP-binding protein rbsa | protein | 506 | 37% helix, 25% strand | Q11C01 |
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 | 546 | 0.72 | 0.80 | 50 | empty |
| 2 | 409 | 0.60 | 0.76 | 40 | empty |
| 3 | 127 | 0.51 | 0.80 | 22 | empty |
| 4 | 93 | 0.38 | 0.76 | 23 | empty |
| 5 | 76 | 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 Q11C01
- Elsewhere: UniProt Q11C01 · AlphaFold DB Q11C01
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