Research workbench
AlphaFold monomer V2.0 prediction for protein root hair defective 3 homolog 2 (Q9FKE9)
Analyse AlphaFold monomer V2.0 prediction for protein root hair defective 3 homolog 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FKE9
- Type
- protein
- Length
- 834 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Protein root hair defective 3 homolog 2
- UniProt
- Q9FKE9
- Pockets
- 7 · best druggability 0.74
Structure
1 distinct chain · 59% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein root hair defective 3 homolog 2 | protein | 834 | 59% helix, 6% strand | Q9FKE9 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.74 | 0.98 | 24 | empty |
| 2 | 133 | 0.58 | 0.84 | 27 | empty |
| 3 | 70 | 0.36 | 0.77 | 15 | empty |
| 4 | 65 | 0.31 | 0.75 | 15 | empty |
| 5 | 68 | 0.30 | 0.74 | 14 | empty |
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 Q9FKE9
- Elsewhere: UniProt Q9FKE9 · AlphaFold DB Q9FKE9
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