MolNFT v1 · #304190 · protein
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A5FQT2)
A5FQT2: “AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (A5FQT2)”. 4 pockets (best druggability 0.78). MolNFT v1 #304190 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A5FQT2
- Type
- protein
- Length
- 720 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3a04CC4b1EEd60433A5218ce3Fa27E32A78EAeC8
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- A5FQT2
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 720 | 34% helix, 28% strand | A5FQT2 |
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 | 958 | 0.78 | 0.80 | 72 | empty |
| 2 | 592 | 0.65 | 0.76 | 67 | empty |
| 3 | 91 | 0.39 | 0.77 | 16 | empty |
| 4 | 50 | 0.29 | 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 A5FQT2
- Elsewhere: UniProt A5FQT2 · AlphaFold DB A5FQT2
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