Research workbench
AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase 1 (P40054)
Analyse AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P40054
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa61D118041847c825681Dedc6F8f8b4D4289cd58
- Molecule
- D-3-phosphoglycerate dehydrogenase 1
- UniProt
- P40054
- Pockets
- 6 · best druggability 0.63
Structure
1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-3-phosphoglycerate dehydrogenase 1 | protein | 469 | 33% helix, 19% strand | P40054 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.63 | 0.76 | 51 | empty |
| 2 | 129 | 0.45 | 0.77 | 23 | empty |
| 3 | 79 | 0.33 | 0.74 | 13 | empty |
| 4 | 55 | 0.31 | 0.76 | 13 | empty |
| 5 | 70 | 0.31 | 0.74 | 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 P40054
- Elsewhere: UniProt P40054 · AlphaFold DB P40054
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