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AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A6QBH4)
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
- A6QBH4
- Type
- protein
- Length
- 729 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc672026d403F8F9B1631F769bF343e5571d0Bdf3
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A6QBH4
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 729 | 34% helix, 30% strand | A6QBH4 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.77 | 0.79 | 75 | empty |
| 2 | 990 | 0.73 | 0.76 | 67 | empty |
| 3 | 192 | 0.52 | 0.78 | 27 | 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 A6QBH4
- Elsewhere: UniProt A6QBH4 · AlphaFold DB A6QBH4
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