Research workbench
AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase (O33116)
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
- O33116
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x51802EfEA2B3096E715D47EAB15912bA1C3cd6c5
- Molecule
- D-3-phosphoglycerate dehydrogenase
- UniProt
- O33116
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-3-phosphoglycerate dehydrogenase | protein | 528 | 34% helix, 25% strand | O33116 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1195 | 0.74 | 0.77 | 109 | empty |
| 2 | 143 | 0.45 | 0.76 | 28 | empty |
| 3 | 64 | 0.44 | 0.82 | 19 | empty |
| 4 | 50 | 0.31 | 0.77 | 13 | 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 O33116
- Elsewhere: UniProt O33116 · AlphaFold DB O33116
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