Research workbench
AlphaFold monomer V2.0 prediction for phospholipase B-like protein C (Q54M94)
Analyse AlphaFold monomer V2.0 prediction for phospholipase B-like protein C (Q54M94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54M94
- Type
- protein
- Length
- 565 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Phospholipase B-like protein C
- UniProt
- Q54M94
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase B-like protein C | protein | 565 | 32% helix, 21% strand | Q54M94 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.80 | 0.94 | 36 | empty |
| 2 | 259 | 0.54 | 0.76 | 28 | empty |
| 3 | 94 | 0.40 | 0.78 | 22 | empty |
| 4 | 53 | 0.28 | 0.74 | 12 | 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 Q54M94
- Elsewhere: UniProt Q54M94 · AlphaFold DB Q54M94
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