Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylglycerol-- prolipoprotein diacylglyceryl transferase (A4VWT2)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylglycerol-- prolipoprotein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4VWT2
- Type
- protein
- Length
- 267 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- UniProt
- A4VWT2
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 64% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | protein | 267 | 64% helix, 9% strand | A4VWT2 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.77 | 0.79 | 60 | empty |
| 2 | 52 | 0.27 | 0.73 | 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 A4VWT2
- Elsewhere: UniProt A4VWT2 · AlphaFold DB A4VWT2
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