Research workbench
AlphaFold monomer V2.0 prediction for 4-hydroxythreonine-4-phosphate dehydrogenase (B4SK42)
Analyse AlphaFold monomer V2.0 prediction for 4-hydroxythreonine-4-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4SK42
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- 4-hydroxythreonine-4-phosphate dehydrogenase
- UniProt
- B4SK42
- Pockets
- 3 · best druggability 0.57
Structure
1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxythreonine-4-phosphate dehydrogenase | protein | 326 | 44% helix, 18% strand | B4SK42 |
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 | 328 | 0.57 | 0.76 | 39 | empty |
| 2 | 122 | 0.55 | 0.83 | 20 | empty |
| 3 | 57 | 0.31 | 0.76 | 12 | 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 B4SK42
- Elsewhere: UniProt B4SK42 · AlphaFold DB B4SK42
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