Research workbench
AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase subunit 1 (A1ST27)
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
- A1ST27
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Sulfate adenylyltransferase subunit 1
- UniProt
- A1ST27
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfate adenylyltransferase subunit 1 | protein | 469 | 26% helix, 32% strand | A1ST27 |
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 | 649 | 0.67 | 0.76 | 76 | empty |
| 2 | 253 | 0.58 | 0.78 | 39 | empty |
| 3 | 58 | 0.26 | 0.72 | 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 A1ST27
- Elsewhere: UniProt A1ST27 · AlphaFold DB A1ST27
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