Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A9WPX4)
Analyse AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9WPX4
- Type
- protein
- Length
- 746 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x619F51Fb686eB178E60C23E8610260c3C69601D6
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A9WPX4
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 746 | 34% helix, 31% strand | A9WPX4 |
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 | 803 | 0.80 | 0.83 | 78 | empty |
| 2 | 565 | 0.68 | 0.78 | 64 | empty |
| 3 | 143 | 0.41 | 0.74 | 19 | empty |
| 4 | 53 | 0.34 | 0.79 | 15 | 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 A9WPX4
- Elsewhere: UniProt A9WPX4 · AlphaFold DB A9WPX4
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