Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9QZH3)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9QZH3
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29f94Aa16B0d73876D150F17c60A3E2f57E61933
- Molecule
- Peptidyl-prolyl cis-trans isomerase E
- UniProt
- Q9QZH3
- Pockets
- 3 · best druggability 0.57
Structure
1 distinct chain · 19% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase E | protein | 301 | 19% helix, 27% strand | Q9QZH3 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.57 | 0.76 | 43 | empty |
| 2 | 98 | 0.40 | 0.77 | 21 | empty |
| 3 | 76 | 0.40 | 0.78 | 15 | empty |
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 Q9QZH3
- Elsewhere: UniProt Q9QZH3 · AlphaFold DB Q9QZH3
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