Research workbench
AlphaFold monomer V2.0 prediction for prostaglandin F2-alpha receptor (Q28905)
Analyse AlphaFold monomer V2.0 prediction for prostaglandin F2-alpha receptor (Q28905) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q28905
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0c3BD61770FeF3aB621008259DC933f6DfDc3882
- Molecule
- Prostaglandin F2-alpha receptor
- UniProt
- Q28905
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin F2-alpha receptor | protein | 362 | 74% helix, 1% strand | Q28905 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.81 | 0.96 | 27 | empty |
| 2 | 508 | 0.70 | 0.80 | 42 | empty |
| 3 | 58 | 0.40 | 0.81 | 18 | empty |
| 4 | 96 | 0.35 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 2 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 Q28905
- Elsewhere: UniProt Q28905 · AlphaFold DB Q28905
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