Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (B1I393)
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
- B1I393
- Type
- protein
- Length
- 741 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- B1I393
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 741 | 34% helix, 28% strand | B1I393 |
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 | 904 | 0.79 | 0.81 | 75 | empty |
| 2 | 830 | 0.69 | 0.76 | 82 | empty |
| 3 | 58 | 0.36 | 0.78 | 12 | empty |
| 4 | 59 | 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 B1I393
- Elsewhere: UniProt B1I393 · AlphaFold DB B1I393
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