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1MZW

Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide

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
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0006457biological_processprotein folding
A0008380biological_processRNA splicing
A0016018molecular_functioncyclosporin A binding
A0016607cellular_componentnuclear speck
A0016853molecular_functionisomerase activity
A0043021molecular_functionribonucleoprotein complex binding
A0045070biological_processpositive regulation of viral genome replication
A0046540cellular_componentU4/U6 x U5 tri-snRNP complex
A0065003biological_processprotein-containing complex assembly
A0071001cellular_componentU4/U6 snRNP
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIkdFMiQGG
ChainResidueDetails
ATYR60-GLY77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues162
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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