Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A4WEX9)
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
- A4WEX9
- Type
- protein
- Length
- 711 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6210d44A4915BD5e50Be1f4196Df3F7d8ebD63e8
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A4WEX9
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 711 | 35% helix, 29% strand | A4WEX9 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 980 | 0.76 | 0.79 | 97 | empty |
| 2 | 832 | 0.69 | 0.76 | 88 | empty |
| 3 | 54 | 0.34 | 0.78 | 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 A4WEX9
- Elsewhere: UniProt A4WEX9 · AlphaFold DB A4WEX9
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