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3PMP

Crystal Structure of Cyclophilin A from Moniliophthora perniciosa in complex with Cyclosporin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR CHAIN C OF CYCLOSPORIN A
ChainResidue
CMLE2
CMLE3
CALA11
CHOH101
CHOH104

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR CHAIN D OF CYCLOSPORIN A
ChainResidue
BLYS32
BARG53
BPHE58
BGLN61
BGLY70
BTYR77
BALA99
BASN100
BALA101
BGLN109
BPHE111
BTRP119
BHIS124
CABA6
CSAR7
CMLE8
DHOH101
DHOH102
ATHR71
AGLU79
AHOH320
BLYS29

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkdSiFHRVIpqFMlQGG
ChainResidueDetails
ATYR46-GLY63

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PDB entries from 2024-07-24

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