7Q6P

Crystal Structure of bacterial Prolyl Peptidyl Isomerase with 5,5'-difluoroleucines

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	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0003824	molecular_function	catalytic activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
D	0000413	biological_process	protein peptidyl-prolyl isomerization
D	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
D	0003824	molecular_function	catalytic activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	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. YnnTiFHRVIngFMiQGG

Chain	Residue	Details
A	TYR36-GLY53

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