Research workbench
AlphaFold monomer V2.0 prediction for sphingomyelinase D (C4JUE5)
Analyse AlphaFold monomer V2.0 prediction for sphingomyelinase D (C4JUE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C4JUE5
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Sphingomyelinase D
- UniProt
- C4JUE5
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sphingomyelinase D | protein | 349 | 38% helix, 17% strand | C4JUE5 |
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 | 186 | 0.67 | 0.86 | 31 | empty |
| 2 | 126 | 0.52 | 0.81 | 23 | empty |
| 3 | 115 | 0.48 | 0.79 | 15 | empty |
| 4 | 58 | 0.31 | 0.76 | 13 | 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 C4JUE5
- Elsewhere: UniProt C4JUE5 · AlphaFold DB C4JUE5
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