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1W74

X-ray structure of peptidyl-prolyl cis-trans isomerase A, PpiA, Rv0009, from Mycobacterium tuberculosis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0009274cellular_componentpeptidoglycan-based cell wall
A0010039biological_processresponse to iron ion
A0016853molecular_functionisomerase activity
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0009274cellular_componentpeptidoglycan-based cell wall
B0010039biological_processresponse to iron ion
B0016853molecular_functionisomerase activity
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YdgAvFHRVIqgFMiQGG
ChainResidueDetails
ATYR66-GLY83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues336
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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