Research workbench
AlphaFold monomer V2.0 prediction for RNA polymerase II-associated protein 3 (Q6NU95)
Analyse AlphaFold monomer V2.0 prediction for RNA polymerase II-associated protein 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6NU95
- Type
- protein
- Length
- 660 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- RNA polymerase II-associated protein 3
- UniProt
- Q6NU95
- Pockets
- 2 · best druggability 0.67
Structure
1 distinct chain · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II-associated protein 3 | protein | 660 | 59% helix, 0% strand | Q6NU95 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 391 | 0.67 | 0.80 | 41 | empty |
| 2 | 63 | 0.31 | 0.75 | 14 | 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 Q6NU95
- Elsewhere: UniProt Q6NU95 · AlphaFold DB Q6NU95
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