Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (P50849)
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
- P50849
- Type
- protein
- Length
- 705 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1D13238705fb34ec8C07e3f58BEEdc523D01E2Ae
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- P50849
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 705 | 37% helix, 29% strand | P50849 |
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 | 1010 | 0.79 | 0.81 | 77 | empty |
| 2 | 606 | 0.64 | 0.75 | 64 | empty |
| 3 | 120 | 0.48 | 0.79 | 20 | empty |
| 4 | 53 | 0.28 | 0.75 | 15 | 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 P50849
- Elsewhere: UniProt P50849 · AlphaFold DB P50849
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