Research workbench
The crystal structure of PPIL1 in complex with cyclosporine a suggests a binding mode for skip
Analyse The crystal structure of PPIL1 in complex with cyclosporine a suggests a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X7K
- Type
- protein
- Length
- 175 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase-like 1; Cyclosporin a
- EC
- 5.2.1.8
- UniProt
- Q9Y3C6
- Ligands
- CD, NA
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase-like 1 (EC 5.2.1.8) | protein | 164 | 14% helix, 30% strand | Q9Y3C6 |
| B | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 491 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 2X7K · The crystal structure of PPIL1 in complex with cyclosporine A suggests a binding mode for… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y3C6 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase-like 1 (Q9Y3C6) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9Y3C6
- Elsewhere: RCSB PDB 2X7K · PDBe 2X7K · UniProt Q9Y3C6
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