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2NUL

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0016853molecular_functionisomerase activity
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues161
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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