Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (C6E2P5)
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
- C6E2P5
- Type
- protein
- Length
- 696 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- C6E2P5
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 696 | 34% helix, 30% strand | C6E2P5 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 891 | 0.74 | 0.78 | 70 | empty |
| 2 | 367 | 0.54 | 0.74 | 33 | empty |
| 3 | 149 | 0.47 | 0.78 | 31 | empty |
| 4 | 71 | 0.39 | 0.79 | 19 | empty |
| 5 | 51 | 0.28 | 0.75 | 13 | 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 C6E2P5
- Elsewhere: UniProt C6E2P5 · AlphaFold DB C6E2P5
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