Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A9ND62)
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
- A9ND62
- Type
- protein
- Length
- 696 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7668FFA4b072bCED36311537cB110Dc7DA447677
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A9ND62
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 696 | 35% helix, 30% strand | A9ND62 |
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 | 891 | 0.76 | 0.79 | 85 | empty |
| 2 | 833 | 0.69 | 0.75 | 74 | empty |
| 3 | 72 | 0.33 | 0.75 | 17 | empty |
| 4 | 73 | 0.32 | 0.75 | 16 | 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 A9ND62
- Elsewhere: UniProt A9ND62 · AlphaFold DB A9ND62
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