Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (B8E2S5)
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
- B8E2S5
- Type
- protein
- Length
- 693 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- B8E2S5
- Pockets
- 6 · best druggability 0.77
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 693 | 35% helix, 30% strand | B8E2S5 |
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 | 782 | 0.77 | 0.81 | 45 | empty |
| 2 | 978 | 0.73 | 0.76 | 74 | empty |
| 3 | 143 | 0.45 | 0.76 | 17 | empty |
| 4 | 107 | 0.41 | 0.76 | 16 | empty |
| 5 | 66 | 0.37 | 0.78 | 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 B8E2S5
- Elsewhere: UniProt B8E2S5 · AlphaFold DB B8E2S5
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