Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A2RMS5)
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
- A2RMS5
- Type
- protein
- Length
- 766 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A2RMS5
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 766 | 33% helix, 27% strand | A2RMS5 |
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 | 989 | 0.76 | 0.78 | 72 | empty |
| 2 | 862 | 0.68 | 0.74 | 68 | empty |
| 3 | 65 | 0.30 | 0.74 | 12 | empty |
| 4 | 56 | 0.26 | 0.73 | 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 A2RMS5
- Elsewhere: UniProt A2RMS5 · AlphaFold DB A2RMS5
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