Research workbench
AlphaFold monomer V2.0 prediction for receptor-like protein 12 (Q9C9H7)
Analyse AlphaFold monomer V2.0 prediction for receptor-like protein 12 (Q9C9H7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C9H7
- Type
- protein
- Length
- 847 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Receptor-like protein 12
- UniProt
- Q9C9H7
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 22% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-like protein 12 | protein | 847 | 22% helix, 23% strand | Q9C9H7 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.67 | 0.81 | 51 | empty |
| 2 | 286 | 0.54 | 0.75 | 41 | empty |
| 3 | 66 | 0.51 | 0.86 | 20 | empty |
| 4 | 51 | 0.30 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 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 Q9C9H7
- Elsewhere: UniProt Q9C9H7 · AlphaFold DB Q9C9H7
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