Research workbench
AlphaFold monomer V2.0 prediction for inactive phospholipase D5 (Q8N7P1)
Analyse AlphaFold monomer V2.0 prediction for inactive phospholipase D5 (Q8N7P1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8N7P1
- Type
- protein
- Length
- 536 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa8003B255b9AFb24F952260d92Ca9AeCD5E715B2
- Molecule
- Inactive phospholipase D5
- UniProt
- Q8N7P1
- Pockets
- 4 · best druggability 0.63
Structure
1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inactive phospholipase D5 | protein | 536 | 33% helix, 22% strand | Q8N7P1 |
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 | 414 | 0.63 | 0.77 | 34 | empty |
| 2 | 238 | 0.49 | 0.75 | 41 | empty |
| 3 | 201 | 0.47 | 0.75 | 32 | empty |
| 4 | 59 | 0.40 | 0.81 | 16 | empty |
Modifications
Observed in the structure: 4 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 Q8N7P1
- Elsewhere: UniProt Q8N7P1 · AlphaFold DB Q8N7P1
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