Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (Q87M06)
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
- Q87M06
- Type
- protein
- Length
- 711 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEFBFDD7c5CFB5252F9d95cDFb437Cf72c1e15430
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- Q87M06
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 711 | 34% helix, 29% strand | Q87M06 |
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 | 882 | 0.76 | 0.79 | 83 | empty |
| 2 | 799 | 0.68 | 0.75 | 71 | empty |
| 3 | 109 | 0.35 | 0.73 | 17 | empty |
| 4 | 78 | 0.34 | 0.75 | 18 | 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 Q87M06
- Elsewhere: UniProt Q87M06 · AlphaFold DB Q87M06
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