Research workbench
AlphaFold monomer V2.0 prediction for pi-plc X domain-containing protein AT5G67130 (Q93XX5)
Analyse AlphaFold monomer V2.0 prediction for pi-plc X domain-containing protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q93XX5
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Pi-plc X domain-containing protein AT5G67130
- UniProt
- Q93XX5
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pi-plc X domain-containing protein AT5G67130 | protein | 426 | 33% helix, 18% strand | Q93XX5 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.60 | 0.78 | 49 | empty |
| 2 | 199 | 0.52 | 0.78 | 32 | empty |
| 3 | 235 | 0.51 | 0.75 | 34 | empty |
| 4 | 60 | 0.33 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 Q93XX5
- Elsewhere: UniProt Q93XX5 · AlphaFold DB Q93XX5
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