Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (Q1IF39)
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
- Q1IF39
- Type
- protein
- Length
- 701 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd2208ADFE78260e78DbEFCf5D704c8D5Ac75625B
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- Q1IF39
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 701 | 34% helix, 30% strand | Q1IF39 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.75 | 0.79 | 80 | empty |
| 2 | 639 | 0.65 | 0.75 | 70 | empty |
| 3 | 88 | 0.54 | 0.85 | 22 | empty |
| 4 | 50 | 0.34 | 0.79 | 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 Q1IF39
- Elsewhere: UniProt Q1IF39 · AlphaFold DB Q1IF39
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