Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q26516)
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
- Q26516
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x14De9B50550E2173e0C98fD70505d1A94f47f847
- Molecule
- Peptidyl-prolyl cis-trans isomerase E
- UniProt
- Q26516
- Pockets
- 2 · best druggability 0.31
Structure
1 distinct chain · 20% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase E | protein | 179 | 20% helix, 30% strand | Q26516 |
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 | 59 | 0.31 | 0.76 | 16 | empty |
| 2 | 51 | 0.30 | 0.76 | 12 | 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 Q26516
- Elsewhere: UniProt Q26516 · AlphaFold DB Q26516
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