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AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A0JUV8)
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
- A0JUV8
- Type
- protein
- Length
- 746 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A0JUV8
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 746 | 34% helix, 31% strand | A0JUV8 |
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 | 952 | 0.78 | 0.80 | 76 | empty |
| 2 | 752 | 0.68 | 0.76 | 70 | empty |
| 3 | 179 | 0.47 | 0.75 | 24 | empty |
| 4 | 64 | 0.36 | 0.78 | 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 A0JUV8
- Elsewhere: UniProt A0JUV8 · AlphaFold DB A0JUV8
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