Research workbench
AlphaFold monomer V2.0 prediction for RNA polymerase II subunit a C-terminal domain phosphatase SSU72 (Q6FMU7)
Analyse AlphaFold monomer V2.0 prediction for RNA polymerase II subunit a C-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6FMU7
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- RNA polymerase II subunit a C-terminal domain phosphatase SSU72
- UniProt
- Q6FMU7
- Pockets
- 2 · best druggability 0.34
Structure
1 distinct chain · 49% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II subunit a C-terminal domain phosphatase SSU72 | protein | 204 | 49% helix, 21% strand | Q6FMU7 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.34 | 0.76 | 22 | empty |
| 2 | 82 | 0.33 | 0.74 | 17 | 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 Q6FMU7
- Elsewhere: UniProt Q6FMU7 · AlphaFold DB Q6FMU7
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