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AlphaFold monomer V2.0 prediction for tuliposide a-converting enzyme B1, amyloplastic (R4X244)
Analyse AlphaFold monomer V2.0 prediction for tuliposide a-converting enzyme B1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- R4X244
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Tuliposide a-converting enzyme B1, amyloplastic
- UniProt
- R4X244
- Pockets
- 4 · best druggability 0.55
Structure
1 distinct chain · 26% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tuliposide a-converting enzyme B1, amyloplastic | protein | 374 | 26% helix, 19% strand | R4X244 |
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 | 339 | 0.55 | 0.75 | 35 | empty |
| 2 | 103 | 0.46 | 0.79 | 22 | empty |
| 3 | 143 | 0.41 | 0.74 | 19 | empty |
| 4 | 105 | 0.37 | 0.74 | 24 | empty |
Modifications
Observed in the structure: 1 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 R4X244
- Elsewhere: UniProt R4X244 · AlphaFold DB R4X244
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