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2K7N

Solution structure of the PPIL1 bound to a fragment of SKIP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000398biological_processmRNA splicing, via spliceosome
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005681cellular_componentspliceosomal complex
A0006397biological_processmRNA processing
A0006457biological_processprotein folding
A0008380biological_processRNA splicing
A0016853molecular_functionisomerase activity
A0071007cellular_componentU2-type catalytic step 2 spliceosome
A0071013cellular_componentcatalytic step 2 spliceosome
A0097718molecular_functiondisordered domain specific binding
A1990403biological_processembryonic brain development
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngTkFHRIIkdFMiQGG
ChainResidueDetails
ATYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues154
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues23
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16595688","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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