Research workbench
AlphaFold monomer V2.0 prediction for bacteriophage adsorption protein B (P0AFA5)
Analyse AlphaFold monomer V2.0 prediction for bacteriophage adsorption protein B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AFA5
- Type
- protein
- Length
- 745 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Bacteriophage adsorption protein B
- UniProt
- P0AFA5
- Pockets
- 7 · best druggability 0.88
Structure
1 distinct chain · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacteriophage adsorption protein B | protein | 745 | 58% helix, 8% strand | P0AFA5 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.88 | 0.89 | 88 | empty |
| 2 | 875 | 0.78 | 0.81 | 66 | empty |
| 3 | 543 | 0.72 | 0.80 | 36 | empty |
| 4 | 503 | 0.61 | 0.75 | 50 | empty |
| 5 | 347 | 0.57 | 0.76 | 35 | 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 P0AFA5
- Elsewhere: UniProt P0AFA5 · AlphaFold DB P0AFA5
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