Research workbench
AlphaFold monomer V2.0 prediction for DNA mismatch repair protein muts (Q12VC9)
Analyse AlphaFold monomer V2.0 prediction for DNA mismatch repair protein muts (Q12VC9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12VC9
- Type
- protein
- Length
- 887 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- DNA mismatch repair protein muts
- UniProt
- Q12VC9
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA mismatch repair protein muts | protein | 887 | 48% helix, 18% strand | Q12VC9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.79 | 0.81 | 115 | empty |
| 2 | 501 | 0.65 | 0.77 | 36 | empty |
| 3 | 128 | 0.41 | 0.75 | 21 | empty |
| 4 | 82 | 0.37 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q12VC9
- Elsewhere: UniProt Q12VC9 · AlphaFold DB Q12VC9
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