Research workbench
AlphaFold monomer V2.0 prediction for smoothened homolog (P56726)
Analyse AlphaFold monomer V2.0 prediction for smoothened homolog (P56726) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P56726
- Type
- protein
- Length
- 793 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8Ef6Fe775853D27970310290fE71Cab5274ae116
- Molecule
- Smoothened homolog
- UniProt
- P56726
- Pockets
- 7 · best druggability 0.81
Structure
1 distinct chain · 45% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Smoothened homolog | protein | 793 | 45% helix, 5% strand | P56726 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.81 | 0.89 | 38 | empty |
| 2 | 654 | 0.65 | 0.75 | 69 | empty |
| 3 | 250 | 0.63 | 0.81 | 34 | empty |
| 4 | 168 | 0.46 | 0.76 | 24 | empty |
| 5 | 79 | 0.37 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 6O3C · Crystal structure of active Smoothened bound to SAG21k, cholesterol, and NbSmo8 · an experimental structure of the same protein · chain A against A, TM-score 0.59
- 6O3C · Crystal structure of active smoothened bound to SAG21K, cholesterol, and NBSMO8 · an experimental structure of the same protein · chain A against A, TM-score 0.59
- 8CXO · Cryo-EM structure of the unliganded mSMO-PGS2 in a lipidic environment · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 8CXO · Cryo-EM structure of the unliganded msmo-PGS2 in a lipidic environment · an experimental structure of the same protein · chain A against A, TM-score 0.44
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 P56726
- Elsewhere: UniProt P56726 · AlphaFold DB P56726
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