Research workbench
AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase (P0A9T2)
Analyse AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A9T2
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- D-3-phosphoglycerate dehydrogenase
- UniProt
- P0A9T2
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-3-phosphoglycerate dehydrogenase | protein | 410 | 34% helix, 20% strand | P0A9T2 |
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 | 633 | 0.67 | 0.77 | 64 | empty |
| 2 | 112 | 0.44 | 0.78 | 26 | empty |
| 3 | 60 | 0.33 | 0.76 | 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 P0A9T2
- Elsewhere: UniProt P0A9T2 · AlphaFold DB P0A9T2
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