Research workbench
AlphaFold monomer V2.0 prediction for cytosolic sulfotransferase 12 (P52839)
Analyse AlphaFold monomer V2.0 prediction for cytosolic sulfotransferase 12 (P52839) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52839
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Cytosolic sulfotransferase 12
- UniProt
- P52839
- Pockets
- 3 · best druggability 0.84
Structure
1 distinct chain · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosolic sulfotransferase 12 | protein | 326 | 49% helix, 10% strand | P52839 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.84 | 0.92 | 60 | empty |
| 2 | 61 | 0.35 | 0.77 | 13 | empty |
| 3 | 54 | 0.26 | 0.73 | 14 | empty |
Compared structures
- 1Q44 · Crystal Structure of an Arabidopsis Thaliana Putative Steroid Sulfotransferase · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 1Q44 · Crystal structure of an arabidopsis thaliana putative steroid sulfotransferase · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 2Q3M · Ensemble refinement of the protein crystal structure of an Arabidopsis thaliana putative… · an experimental structure of the same protein · chain A against A, TM-score 0.80
- 2Q3M · Ensemble refinement of the protein crystal structure of an arabidopsis thaliana putative… · an experimental structure of the same protein · chain A against A, TM-score 0.80
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 P52839
- Elsewhere: UniProt P52839 · AlphaFold DB P52839
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