Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase nima-interacting 1 (Q9QUR7)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9QUR7
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0F7aAe0F58509eB3BaA013d642d748C7C38B0F93
- Molecule
- Peptidyl-prolyl cis-trans isomerase nima-interacting 1
- UniProt
- Q9QUR7
- Pockets
- 2 · best druggability 0.33
Structure
1 distinct chain · 24% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 | protein | 165 | 24% helix, 22% strand | Q9QUR7 |
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 | 77 | 0.33 | 0.74 | 20 | empty |
| 2 | 84 | 0.32 | 0.74 | 20 | 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 Q9QUR7
- Elsewhere: UniProt Q9QUR7 · AlphaFold DB Q9QUR7
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