Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A9BH73)
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
- A9BH73
- Type
- protein
- Length
- 695 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x02ba1297E099E2bE241b90eF8A279dBA8073B098
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A9BH73
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 695 | 36% helix, 29% strand | A9BH73 |
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 | 754 | 0.75 | 0.80 | 71 | empty |
| 2 | 641 | 0.64 | 0.74 | 66 | empty |
| 3 | 124 | 0.39 | 0.74 | 21 | empty |
| 4 | 58 | 0.26 | 0.72 | 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 A9BH73
- Elsewhere: UniProt A9BH73 · AlphaFold DB A9BH73
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