Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A4XYD6)
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
- A4XYD6
- Type
- protein
- Length
- 702 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A4XYD6
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 702 | 34% helix, 30% strand | A4XYD6 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.76 | 0.80 | 76 | empty |
| 2 | 567 | 0.63 | 0.75 | 56 | empty |
| 3 | 67 | 0.55 | 0.88 | 19 | empty |
| 4 | 52 | 0.33 | 0.78 | 15 | empty |
| 5 | 54 | 0.31 | 0.77 | 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 A4XYD6
- Elsewhere: UniProt A4XYD6 · AlphaFold DB A4XYD6
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