Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (C1F8M1)
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
- C1F8M1
- Type
- protein
- Length
- 806 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- C1F8M1
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 806 | 31% helix, 27% strand | C1F8M1 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1147 | 0.76 | 0.79 | 76 | empty |
| 2 | 595 | 0.64 | 0.75 | 56 | empty |
| 3 | 106 | 0.56 | 0.85 | 23 | empty |
| 4 | 73 | 0.45 | 0.82 | 22 | empty |
| 5 | 56 | 0.36 | 0.79 | 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 C1F8M1
- Elsewhere: UniProt C1F8M1 · AlphaFold DB C1F8M1
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