2RMC

Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0006457	biological_process	protein folding
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0006457	biological_process	protein folding
E	0000413	biological_process	protein peptidyl-prolyl isomerization
E	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
E	0006457	biological_process	protein folding
G	0000413	biological_process	protein peptidyl-prolyl isomerization
G	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
G	0006457	biological_process	protein folding

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgSiFHRVIkdFMiQGG

Chain	Residue	Details
A	TYR82-GLY99

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	628
Details	Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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