Research workbench
AlphaFold monomer V2.0 prediction for prostaglandin G/H synthase 1 (P23219)
Analyse AlphaFold monomer V2.0 prediction for prostaglandin G/H synthase 1 (P23219) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23219
- Type
- protein
- Length
- 599 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Prostaglandin G/H synthase 1
- UniProt
- P23219
- Pockets
- 6 · best druggability 0.78
Structure
1 distinct chain · 44% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin G/H synthase 1 | protein | 599 | 44% helix, 8% strand | P23219 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.78 | 0.80 | 94 | empty |
| 2 | 390 | 0.67 | 0.80 | 36 | empty |
| 3 | 158 | 0.40 | 0.73 | 27 | empty |
| 4 | 81 | 0.32 | 0.74 | 20 | empty |
| 5 | 55 | 0.27 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6Y3C · Human COX-1 crystal structure · an experimental structure of the same protein · chain A against A, TM-score 0.93
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 P23219
- Elsewhere: UniProt P23219 · AlphaFold DB P23219
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