Research workbench
AlphaFold monomer V2.0 prediction for formyl peptide receptor-related sequence 4 (A4FUQ5)
Analyse AlphaFold monomer V2.0 prediction for formyl peptide receptor-related sequence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4FUQ5
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Formyl peptide receptor-related sequence 4
- UniProt
- A4FUQ5
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 82% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formyl peptide receptor-related sequence 4 | protein | 323 | 82% helix, 3% strand | A4FUQ5 |
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 | 1200 | 0.75 | 0.77 | 79 | empty |
| 2 | 187 | 0.63 | 0.83 | 21 | empty |
| 3 | 96 | 0.59 | 0.87 | 17 | empty |
| 4 | 55 | 0.32 | 0.76 | 13 | empty |
| 5 | 60 | 0.30 | 0.74 | 13 | 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 A4FUQ5
- Elsewhere: UniProt A4FUQ5 · AlphaFold DB A4FUQ5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.