Research workbench
AlphaFold monomer V2.0 prediction for selenium-binding protein 1 (O23264)
Analyse AlphaFold monomer V2.0 prediction for selenium-binding protein 1 (O23264) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O23264
- Type
- protein
- Length
- 490 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6e687cC6e263D2A00FeB863E3480af514fBBF1Bd
- Molecule
- Selenium-binding protein 1
- UniProt
- O23264
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Selenium-binding protein 1 | protein | 490 | 10% helix, 37% strand | O23264 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.45 | 0.75 | 22 | empty |
| 2 | 69 | 0.43 | 0.80 | 17 | empty |
| 3 | 53 | 0.29 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 O23264
- Elsewhere: UniProt O23264 · AlphaFold DB O23264
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