Research workbench
AlphaFold monomer V2.0 prediction for 3-mercaptopyruvate sulfurtransferase (P31142)
Analyse AlphaFold monomer V2.0 prediction for 3-mercaptopyruvate sulfurtransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P31142
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- 3-mercaptopyruvate sulfurtransferase
- UniProt
- P31142
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 31% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-mercaptopyruvate sulfurtransferase | protein | 281 | 31% helix, 15% strand | P31142 |
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 | 148 | 0.51 | 0.79 | 32 | empty |
| 2 | 119 | 0.42 | 0.76 | 18 | empty |
| 3 | 52 | 0.32 | 0.77 | 13 | empty |
Compared structures
- 1URH · The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases… · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 1URH · The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases… · an experimental structure of the same protein · chain A against A, TM-score 0.89
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 P31142
- Elsewhere: UniProt P31142 · AlphaFold DB P31142
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