Research workbench
AlphaFold monomer V2.0 prediction for protein scarecrow (Q9M384)
Analyse AlphaFold monomer V2.0 prediction for protein scarecrow (Q9M384) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9M384
- Type
- protein
- Length
- 653 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6caDF58687FA86EEd5943cD410b8F963d69C56Dd
- Molecule
- Protein scarecrow
- UniProt
- Q9M384
- Pockets
- 5 · best druggability 0.79
Structure
1 distinct chain · 40% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein scarecrow | protein | 653 | 40% helix, 9% strand | Q9M384 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1143 | 0.79 | 0.81 | 99 | empty |
| 2 | 496 | 0.62 | 0.76 | 47 | empty |
| 3 | 295 | 0.57 | 0.77 | 29 | empty |
| 4 | 68 | 0.49 | 0.84 | 16 | empty |
| 5 | 71 | 0.36 | 0.77 | 10 | empty |
Compared structures
- 5B3G · The crystal structure of the heterodimer of short-root and scarecrow gras domains · an experimental structure of the same protein · chain A against A, TM-score 0.57
- 5B3G · The crystal structure of the heterodimer of SHORT-ROOT and SCARECROW GRAS domains · an experimental structure of the same protein · chain A against A, TM-score 0.57
- 5B3H · The crystal structure of the JACKDAW/IDD10 bound to the heterodimeric shr-scr complex · an experimental structure of the same protein · chain A against A, TM-score 0.56
- 5B3H · The crystal structure of the JACKDAW/IDD10 bound to the heterodimeric SHR-SCR complex · an experimental structure of the same protein · chain A against A, TM-score 0.56
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 Q9M384
- Elsewhere: UniProt Q9M384 · AlphaFold DB Q9M384
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