Research workbench
AlphaFold monomer V2.0 prediction for endonuclease V (B5F1I1)
Analyse AlphaFold monomer V2.0 prediction for endonuclease V (B5F1I1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5F1I1
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80fFD76c298b93E8762b4d46AD7aBea1fcDf9723
- Molecule
- Endonuclease V
- UniProt
- B5F1I1
- Pockets
- 1 · best druggability 0.45
Structure
1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease V | protein | 223 | 31% helix, 27% strand | B5F1I1 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.45 | 0.77 | 23 | 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 B5F1I1
- Elsewhere: UniProt B5F1I1 · AlphaFold DB B5F1I1
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