Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (B1Y823)
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
- B1Y823
- Type
- protein
- Length
- 767 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd6bC1C645b7B141A4643641CCE4f692185f8f8FC
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- B1Y823
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 767 | 32% helix, 26% strand | B1Y823 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.76 | 0.78 | 89 | empty |
| 2 | 977 | 0.71 | 0.75 | 72 | empty |
| 3 | 102 | 0.41 | 0.77 | 24 | 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 B1Y823
- Elsewhere: UniProt B1Y823 · AlphaFold DB B1Y823
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