Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A5CSN9)
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
- A5CSN9
- Type
- protein
- Length
- 757 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A5CSN9
- Pockets
- 5 · best druggability 0.79
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 757 | 34% helix, 30% strand | A5CSN9 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.79 | 0.82 | 77 | empty |
| 2 | 439 | 0.59 | 0.75 | 37 | empty |
| 3 | 158 | 0.50 | 0.78 | 26 | empty |
| 4 | 193 | 0.47 | 0.75 | 26 | empty |
| 5 | 60 | 0.35 | 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 A5CSN9
- Elsewhere: UniProt A5CSN9 · AlphaFold DB A5CSN9
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