Research workbench
AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (A0PZP4)
Analyse AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (A0PZP4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0PZP4
- Type
- protein
- Length
- 785 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Endonuclease MUTS2
- UniProt
- A0PZP4
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease MUTS2 | protein | 785 | 53% helix, 16% strand | A0PZP4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.50 | 0.75 | 37 | empty |
| 2 | 65 | 0.39 | 0.80 | 18 | empty |
| 3 | 76 | 0.34 | 0.75 | 13 | empty |
| 4 | 71 | 0.28 | 0.72 | 14 | 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 A0PZP4
- Elsewhere: UniProt A0PZP4 · AlphaFold DB A0PZP4
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