Research workbench
AlphaFold monomer V2.0 prediction for ribosome-binding ATPase ychf (P0ABU4)
Analyse AlphaFold monomer V2.0 prediction for ribosome-binding ATPase ychf (P0ABU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0ABU4
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Ribosome-binding ATPase ychf
- UniProt
- P0ABU4
- Pockets
- 5 · best druggability 0.61
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosome-binding ATPase ychf | protein | 363 | 47% helix, 19% strand | P0ABU4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.61 | 0.80 | 21 | empty |
| 2 | 155 | 0.46 | 0.76 | 28 | empty |
| 3 | 164 | 0.42 | 0.74 | 16 | empty |
| 4 | 72 | 0.37 | 0.77 | 19 | empty |
| 5 | 75 | 0.31 | 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 P0ABU4
- Elsewhere: UniProt P0ABU4 · AlphaFold DB P0ABU4
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