Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (O34275)
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
- O34275
- Type
- protein
- Length
- 706 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- O34275
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 706 | 35% helix, 30% strand | O34275 |
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 | 1003 | 0.75 | 0.78 | 95 | empty |
| 2 | 760 | 0.67 | 0.75 | 79 | empty |
| 3 | 58 | 0.34 | 0.77 | 14 | empty |
| 4 | 53 | 0.29 | 0.75 | 17 | 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 O34275
- Elsewhere: UniProt O34275 · AlphaFold DB O34275
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