Research workbench
AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (C4XS37)
Analyse AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (C4XS37) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C4XS37
- Type
- protein
- Length
- 773 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Endonuclease MUTS2
- UniProt
- C4XS37
- Pockets
- 5 · best druggability 0.40
Structure
1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease MUTS2 | protein | 773 | 51% helix, 16% strand | C4XS37 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.40 | 0.77 | 21 | empty |
| 2 | 118 | 0.38 | 0.74 | 17 | empty |
| 3 | 79 | 0.34 | 0.75 | 16 | empty |
| 4 | 50 | 0.26 | 0.74 | 11 | empty |
| 5 | 51 | 0.25 | 0.73 | 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 C4XS37
- Elsewhere: UniProt C4XS37 · AlphaFold DB C4XS37
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