Research workbench
AlphaFold monomer V2.0 prediction for D-3-phosphoglycerate dehydrogenase (P0A545)
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
- P0A545
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8e3a917A16E8163577aA515EA010E513A6d710df
- Molecule
- D-3-phosphoglycerate dehydrogenase
- UniProt
- P0A545
- Pockets
- 3 · best druggability 0.75
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 | P0A545 |
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 | 1066 | 0.75 | 0.77 | 96 | empty |
| 2 | 82 | 0.41 | 0.79 | 22 | empty |
| 3 | 127 | 0.38 | 0.73 | 26 | 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 P0A545
- Elsewhere: UniProt P0A545 · AlphaFold DB P0A545
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