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2OJU

X-ray structure of complex of human cyclophilin J with cyclosporin A

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
A0016853molecular_functionisomerase activity
A0071013cellular_componentcatalytic step 2 spliceosome
B0000398biological_processmRNA splicing, via spliceosome
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005681cellular_componentspliceosomal complex
B0006397biological_processmRNA processing
B0006457biological_processprotein folding
B0008380biological_processRNA splicing
B0016853molecular_functionisomerase activity
B0071013cellular_componentcatalytic step 2 spliceosome
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR CHAIN C OF CYCLOSPORIN A
ChainResidue
AGLU32
AASN98
AGLN106
APHE108
AHIS116
ATYR121
APRO164
AHOH2003
BSER1
BVAL3
CHOH2001
AALA36
AALA39
AARG50
APHE55
AGLN58
AGLY66
AALA96
AASN97

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR CHAIN D OF CYCLOSPORIN A
ChainResidue
BLEU35
BALA36
BALA39
BSER40
BARG50
BPHE55
BGLN58
BGLY66
BARG67
BALA96
BASN97
BASN98
BGLN106
BPHE108
BHIS116
BTYR121
BHOH2004

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngCiFHRNIkgFMvQTG
ChainResidueDetails
ATYR43-GLY60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER8
BSER8

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q9D6L8
ChainResidueDetails
AARG67
BARG67

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PDB entries from 2025-06-18

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