Research workbench
AlphaFold monomer V2.0 prediction for exonuclease V, mitochondrial (C5DXZ1)
Analyse AlphaFold monomer V2.0 prediction for exonuclease V, mitochondrial (C5DXZ1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5DXZ1
- Type
- protein
- Length
- 543 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Exonuclease V, mitochondrial
- UniProt
- C5DXZ1
- Pockets
- 7 · best druggability 0.75
Structure
1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exonuclease V, mitochondrial | protein | 543 | 46% helix, 14% strand | C5DXZ1 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.75 | 0.78 | 58 | empty |
| 2 | 327 | 0.64 | 0.80 | 55 | empty |
| 3 | 54 | 0.47 | 0.85 | 14 | empty |
| 4 | 69 | 0.39 | 0.79 | 12 | empty |
| 5 | 51 | 0.33 | 0.79 | 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 C5DXZ1
- Elsewhere: UniProt C5DXZ1 · AlphaFold DB C5DXZ1
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