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7Q6P

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0061077biological_processchaperone-mediated protein folding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0061077biological_processchaperone-mediated protein folding
C0000413biological_processprotein peptidyl-prolyl isomerization
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0061077biological_processchaperone-mediated protein folding
D0000413biological_processprotein peptidyl-prolyl isomerization
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006457biological_processprotein folding
D0061077biological_processchaperone-mediated protein folding
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YnnTiFHRVIngFMiQGG
ChainResidueDetails
ATYR36-GLY53

221051

PDB entries from 2024-06-12

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