Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (Q83G94)
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
- Q83G94
- Type
- protein
- Length
- 738 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- Q83G94
- Pockets
- 6 · best druggability 0.77
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 738 | 35% helix, 30% strand | Q83G94 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 668 | 0.77 | 0.82 | 76 | empty |
| 2 | 683 | 0.66 | 0.75 | 68 | empty |
| 3 | 89 | 0.36 | 0.75 | 17 | empty |
| 4 | 64 | 0.32 | 0.75 | 18 | empty |
| 5 | 68 | 0.30 | 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 Q83G94
- Elsewhere: UniProt Q83G94 · AlphaFold DB Q83G94
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