Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase D (Q9CR16)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CR16
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Peptidyl-prolyl cis-trans isomerase D
- UniProt
- Q9CR16
- Pockets
- 1 · best druggability 0.49
Structure
1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase D | protein | 370 | 43% helix, 17% strand | Q9CR16 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.49 | 0.77 | 23 | 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 Q9CR16
- Elsewhere: UniProt Q9CR16 · AlphaFold DB Q9CR16
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