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1XO7

Crystal structure of cyclophilin from Trypanosoma cruzi

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016018molecular_functioncyclosporin A binding
A0016853molecular_functionisomerase activity
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0016018molecular_functioncyclosporin A binding
B0016853molecular_functionisomerase activity
C0000413biological_processprotein peptidyl-prolyl isomerization
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005737cellular_componentcytoplasm
C0006457biological_processprotein folding
C0016018molecular_functioncyclosporin A binding
C0016853molecular_functionisomerase activity
D0000413biological_processprotein peptidyl-prolyl isomerization
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0005737cellular_componentcytoplasm
D0006457biological_processprotein folding
D0016018molecular_functioncyclosporin A binding
D0016853molecular_functionisomerase activity
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgSiFHRVIrnFMiQGG
ChainResidueDetails
ATYR50-GLY67

237992

PDB entries from 2025-06-25

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