Research workbench
AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (A5IMS8)
Analyse AlphaFold monomer V2.0 prediction for endonuclease MUTS2 (A5IMS8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5IMS8
- Type
- protein
- Length
- 757 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6b3373535645884b693Bc933E91A27320E504095
- Molecule
- Endonuclease MUTS2
- UniProt
- A5IMS8
- Pockets
- 4 · best druggability 0.55
Structure
1 distinct chain · 53% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease MUTS2 | protein | 757 | 53% helix, 17% strand | A5IMS8 |
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 | 225 | 0.55 | 0.78 | 39 | empty |
| 2 | 151 | 0.44 | 0.75 | 26 | empty |
| 3 | 125 | 0.40 | 0.75 | 17 | empty |
| 4 | 52 | 0.27 | 0.73 | 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 A5IMS8
- Elsewhere: UniProt A5IMS8 · AlphaFold DB A5IMS8
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