Research workbench
AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase subunit 1 (A6QB12)
Analyse AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6QB12
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2A761b38A61332c74222D3acB8AE18729942078b
- Molecule
- Sulfate adenylyltransferase subunit 1
- UniProt
- A6QB12
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate adenylyltransferase subunit 1 | protein | 479 | 28% helix, 32% strand | A6QB12 |
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 | 772 | 0.70 | 0.76 | 73 | empty |
| 2 | 213 | 0.58 | 0.80 | 32 | empty |
| 3 | 52 | 0.27 | 0.74 | 16 | empty |
| 4 | 54 | 0.26 | 0.73 | 14 | 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 A6QB12
- Elsewhere: UniProt A6QB12 · AlphaFold DB A6QB12
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