Research workbench
AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (O51125)
Analyse AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (O51125) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O51125
- Type
- protein
- Length
- 780 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Endonuclease MUTS2
- UniProt
- O51125
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease MUTS2 | protein | 780 | 54% helix, 15% strand | O51125 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.48 | 0.78 | 19 | empty |
| 2 | 55 | 0.46 | 0.84 | 22 | empty |
| 3 | 71 | 0.33 | 0.76 | 21 | empty |
| 4 | 60 | 0.30 | 0.76 | 13 | 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 O51125
- Elsewhere: UniProt O51125 · AlphaFold DB O51125
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