Research workbench
AlphaFold monomer V2.0 prediction for phospholipase C D (P0A5R9)
Analyse AlphaFold monomer V2.0 prediction for phospholipase C D (P0A5R9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A5R9
- Type
- protein
- Length
- 514 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc1561376793393b1CA847254750D93728aCFE619
- Molecule
- Phospholipase C D
- UniProt
- P0A5R9
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 37% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase C D | protein | 514 | 37% helix, 13% strand | P0A5R9 |
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 | 367 | 0.58 | 0.76 | 54 | empty |
| 2 | 64 | 0.43 | 0.81 | 17 | empty |
| 3 | 57 | 0.26 | 0.73 | 18 | empty |
Modifications
Observed in the structure: 2 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 P0A5R9
- Elsewhere: UniProt P0A5R9 · AlphaFold DB P0A5R9
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