Research workbench
AlphaFold monomer V2.0 prediction for adenylyltransferase and sulfurtransferase UBA4 (Q0CFD4)
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
- Q0CFD4
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0516f45504313116a39Bf19510608C1ee67B38b1
- Molecule
- Adenylyltransferase and sulfurtransferase UBA4
- UniProt
- Q0CFD4
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylyltransferase and sulfurtransferase UBA4 | protein | 484 | 43% helix, 13% strand | Q0CFD4 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.67 | 0.80 | 54 | empty |
| 2 | 335 | 0.60 | 0.78 | 42 | empty |
| 3 | 105 | 0.54 | 0.83 | 17 | empty |
| 4 | 153 | 0.51 | 0.79 | 26 | empty |
| 5 | 57 | 0.41 | 0.82 | 11 | 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 Q0CFD4
- Elsewhere: UniProt Q0CFD4 · AlphaFold DB Q0CFD4
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