Research workbench
AlphaFold monomer V2.0 prediction for ribosome-binding ATPase ychf (Q7VMI2)
Analyse AlphaFold monomer V2.0 prediction for ribosome-binding ATPase ychf (Q7VMI2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7VMI2
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Ribosome-binding ATPase ychf
- UniProt
- Q7VMI2
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosome-binding ATPase ychf | protein | 363 | 46% helix, 19% strand | Q7VMI2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.58 | 0.79 | 23 | empty |
| 2 | 171 | 0.46 | 0.76 | 29 | empty |
| 3 | 161 | 0.44 | 0.75 | 15 | empty |
| 4 | 105 | 0.39 | 0.75 | 25 | 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 Q7VMI2
- Elsewhere: UniProt Q7VMI2 · AlphaFold DB Q7VMI2
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