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1IST

Crystal structure of yeast cyclophilin A, CPR1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003729molecular_functionmRNA binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0006457biological_processprotein folding
A0006974biological_processDNA damage response
A0009267biological_processcellular response to starvation
A0015031biological_processprotein transport
A0016018molecular_functioncyclosporin A binding
A0016853molecular_functionisomerase activity
A0030437biological_processascospore formation
A0034967cellular_componentSet3 complex
A0045835biological_processnegative regulation of meiotic nuclear division
A0045836biological_processpositive regulation of meiotic nuclear division
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003729molecular_functionmRNA binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0006457biological_processprotein folding
B0006974biological_processDNA damage response
B0009267biological_processcellular response to starvation
B0015031biological_processprotein transport
B0016018molecular_functioncyclosporin A binding
B0016853molecular_functionisomerase activity
B0030437biological_processascospore formation
B0034967cellular_componentSet3 complex
B0045835biological_processnegative regulation of meiotic nuclear division
B0045836biological_processpositive regulation of meiotic nuclear division
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YagSpFHRVIpdFMlQGG
ChainResidueDetails
ATYR46-GLY63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues312
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"2687115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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