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AlphaFold monomer V2.0 prediction for high frequency lysogenization protein hfld homolog (B2VDR3)
Analyse AlphaFold monomer V2.0 prediction for high frequency lysogenization protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2VDR3
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x572ca54c59cbee8eDC4B5f2586e33e3f4da57bB0
- Molecule
- High frequency lysogenization protein hfld homolog
- UniProt
- B2VDR3
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High frequency lysogenization protein hfld homolog | protein | 214 | 74% helix, 0% strand | B2VDR3 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.45 | 0.79 | 20 | empty |
| 2 | 70 | 0.41 | 0.79 | 13 | empty |
| 3 | 92 | 0.40 | 0.77 | 12 | 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 B2VDR3
- Elsewhere: UniProt B2VDR3 · AlphaFold DB B2VDR3
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