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AlphaFold monomer V2.0 prediction for receptor homology region, transmembrane domain- and ring domain-containing protein 6 (F4HZZ4)
Analyse AlphaFold monomer V2.0 prediction for receptor homology region, transmembrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F4HZZ4
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4eeFE54a22B1b00963d23684aF0369c867210F7E
- Molecule
- Receptor homology region, transmembrane domain- and ring domain-containing protein 6
- UniProt
- F4HZZ4
- Pockets
- 2 · best druggability 0.43
Structure
1 distinct chain · 28% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor homology region, transmembrane domain- and ring domain-containing protein 6 | protein | 318 | 28% helix, 17% strand | F4HZZ4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.43 | 0.76 | 17 | empty |
| 2 | 71 | 0.33 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 1 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 F4HZZ4
- Elsewhere: UniProt F4HZZ4 · AlphaFold DB F4HZZ4
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