Research workbench
AlphaFold monomer V2.0 prediction for endonuclease V (Q0A5M1)
Analyse AlphaFold monomer V2.0 prediction for endonuclease V (Q0A5M1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0A5M1
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Endonuclease V
- UniProt
- Q0A5M1
- Pockets
- 1 · best druggability 0.50
Structure
1 distinct chain · 26% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease V | protein | 227 | 26% helix, 27% strand | Q0A5M1 |
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 | 145 | 0.50 | 0.79 | 29 | 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 Q0A5M1
- Elsewhere: UniProt Q0A5M1 · AlphaFold DB Q0A5M1
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