Research workbench
AlphaFold monomer V2.0 prediction for adenylyltransferase and sulfurtransferase UBA4 (A5DSR2)
Analyse AlphaFold monomer V2.0 prediction for adenylyltransferase and sulfurtransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5DSR2
- Type
- protein
- Length
- 455 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c7eF5512E51Bcd3d8e1379AFF339AD78CFbD034
- Molecule
- Adenylyltransferase and sulfurtransferase UBA4
- UniProt
- A5DSR2
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylyltransferase and sulfurtransferase UBA4 | protein | 455 | 43% helix, 15% strand | A5DSR2 |
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 | 922 | 0.75 | 0.78 | 93 | empty |
| 2 | 641 | 0.68 | 0.77 | 46 | empty |
| 3 | 64 | 0.37 | 0.78 | 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 A5DSR2
- Elsewhere: UniProt A5DSR2 · AlphaFold DB A5DSR2
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