Research workbench
AlphaFold monomer V2.0 prediction for protein short-root (Q9SZF7)
Analyse AlphaFold monomer V2.0 prediction for protein short-root (Q9SZF7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9SZF7
- Type
- protein
- Length
- 531 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01aba851199Eb07393BDe5cB24AD7B4a1a6998D0
- Molecule
- Protein short-root
- UniProt
- Q9SZF7
- Pockets
- 6 · best druggability 0.84
Structure
1 distinct chain · 43% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein short-root | protein | 531 | 43% helix, 12% strand | Q9SZF7 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1167 | 0.84 | 0.85 | 80 | empty |
| 2 | 126 | 0.76 | 0.94 | 19 | empty |
| 3 | 163 | 0.59 | 0.83 | 29 | empty |
| 4 | 199 | 0.58 | 0.80 | 28 | empty |
| 5 | 71 | 0.37 | 0.77 | 12 | empty |
Compared structures
- 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 B, TM-score 0.76
- 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 B, TM-score 0.76
- 5B3G · The crystal structure of the heterodimer of short-root and scarecrow gras domains · an experimental structure of the same protein · chain A against B, TM-score 0.75
- 5B3G · The crystal structure of the heterodimer of SHORT-ROOT and SCARECROW GRAS domains · an experimental structure of the same protein · chain A against B, TM-score 0.75
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 Q9SZF7
- Elsewhere: UniProt Q9SZF7 · AlphaFold DB Q9SZF7
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