MolNFT v1 · #304208 · protein
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A5EXU0)
A5EXU0: “AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A5EXU0)”. 3 pockets (best druggability 0.74). MolNFT v1 #304208 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A5EXU0
- Type
- protein
- Length
- 693 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A5EXU0
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 693 | 34% helix, 30% strand | A5EXU0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 961 | 0.74 | 0.77 | 78 | empty |
| 2 | 880 | 0.69 | 0.75 | 83 | empty |
| 3 | 50 | 0.34 | 0.79 | 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 A5EXU0
- Elsewhere: UniProt A5EXU0 · AlphaFold DB A5EXU0
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