Research workbench
AlphaFold monomer V2.0 prediction for endonuclease V (Q9YES5)
Analyse AlphaFold monomer V2.0 prediction for endonuclease V (Q9YES5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9YES5
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3CfADCfFEABDd4A50940a7AC50c58466c2A37Aab
- Molecule
- Endonuclease V
- UniProt
- Q9YES5
- Pockets
- 1 · best druggability 0.47
Structure
1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease V | protein | 255 | 30% helix, 30% strand | Q9YES5 |
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 | 164 | 0.47 | 0.77 | 29 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q9YES5
- Elsewhere: UniProt Q9YES5 · AlphaFold DB Q9YES5
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