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AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase nima-interacting 1 (Q4R383)
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
- Q4R383
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Peptidyl-prolyl cis-trans isomerase nima-interacting 1
- UniProt
- Q4R383
- Pockets
- 3 · 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 | 163 | 24% helix, 22% strand | Q4R383 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.33 | 0.75 | 18 | empty |
| 2 | 70 | 0.31 | 0.74 | 17 | empty |
| 3 | 54 | 0.27 | 0.73 | 13 | 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 Q4R383
- Elsewhere: UniProt Q4R383 · AlphaFold DB Q4R383
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