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1QNH

Plasmodium falciparum Cyclophilin (double mutant) complexed with Cyclosporin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016018molecular_functioncyclosporin A binding
A0016853molecular_functionisomerase activity
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0016018molecular_functioncyclosporin A binding
B0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR CHAIN C OF CYCLOSPORIN A
ChainResidue
AARG62
AHIS133
BALA110
CHOH2002
CHOH2003
DBMT205
APHE67
AGLN70
AGLY79
AALA108
AASN109
AGLN118
ALEU120
ATRP128

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR CHAIN D OF CYCLOSPORIN A
ChainResidue
AARG88
AALA110
AHOH2037
BARG62
BPHE67
BGLN70
BGLY79
BALA108
BASN109
BGLN118
BLEU120
BTRP128
BLEU129
BHIS133
CABA206
CSAR207
DHOH2002
DHOH2003
DHOH2004

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YknSiFHRIIpqFMcQGG
ChainResidueDetails
ATYR55-GLY72

239803

PDB entries from 2025-08-06

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