Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A0K927)
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
- A0K927
- Type
- protein
- Length
- 715 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A0K927
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 715 | 36% helix, 29% strand | A0K927 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 828 | 0.73 | 0.78 | 71 | empty |
| 2 | 1053 | 0.70 | 0.75 | 88 | empty |
| 3 | 121 | 0.39 | 0.75 | 24 | empty |
| 4 | 107 | 0.37 | 0.74 | 18 | empty |
| 5 | 52 | 0.27 | 0.74 | 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 A0K927
- Elsewhere: UniProt A0K927 · AlphaFold DB A0K927
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