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1XYH

Crystal Structure of Recombinant Human Cyclophilin J

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
A0005654cellular_componentnucleoplasm
A0005681cellular_componentspliceosomal complex
A0006397biological_processmRNA processing
A0006457biological_processprotein folding
A0008380biological_processRNA splicing
A0071013cellular_componentcatalytic step 2 spliceosome
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngCiFHRNIkgFMvQTG
ChainResidueDetails
ATYR37-GLY54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q9D6L8
ChainResidueDetails
AARG61

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PDB entries from 2024-05-01

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