Crystal structure of peptidyl-prolyl cis-trans isomerase from encephalitozoon cuniculi at 1.9 a resolution

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 30% strand (DSSP).

Ligands and binding sites

• SO4 · Sulfate ion · ion · 2 copies · chains B, C, D
• PG5 · 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane · additive · 2 copies · chains A, C, B
• EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–C · 773 Ų buried · 15 hydrogen bonds · protein-protein
• B–D · 732 Ų buried · 11 hydrogen bonds · protein-protein
• B–C · 403 Ų buried · 1 hydrogen bond · protein-protein
• C–D · 12 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 3K2C · Crystal structure of peptidyl-prolyl cis-trans isomerase from Encephalitozoon cuniculi at… · the same entry in another collection · chain D against D, TM-score 1.00
• Q8SRE1 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase (Q8SRE1) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q8SRE1
• Elsewhere: RCSB PDB 3K2C · PDBe 3K2C · UniProt Q8SRE1