Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase (Q28KD9)
Analyse AlphaFold monomer V2.0 prediction for glycerol-3-phosphate acyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q28KD9
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Glycerol-3-phosphate acyltransferase
- UniProt
- Q28KD9
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate acyltransferase | protein | 203 | 71% helix, 0% strand | Q28KD9 |
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 | 251 | 0.67 | 0.84 | 38 | empty |
| 2 | 57 | 0.32 | 0.76 | 13 | empty |
| 3 | 56 | 0.28 | 0.74 | 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 Q28KD9
- Elsewhere: UniProt Q28KD9 · AlphaFold DB Q28KD9
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