Structure of PDB 1cyn Chain A Binding Site BS01

Receptor Information
>1cyn Chain A (length=178) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGY
KNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWV
SMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTD
SRDKPLKDVIIADCGKIEVEKPFAIAKE
Ligand information
>1cyn Chain C (length=11) Species: 29910 (Tolypocladium inflatum) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ALLVTPGLVLA
Receptor-Ligand Complex Structure
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PDB1cyn X-Ray Structure of a Cyclophilin B/Cyclosporin Complex: Comparison with Cyclophilin a and Delineation of its Calcineurin-Binding Domain.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		R63 F68 Q71 G80 A109 N110 A111 Q119 F121 W129 H134
Binding residue
(residue number reindexed from 1)		R57 F62 Q65 G74 A103 N104 A105 Q113 F115 W123 H128
Enzymatic activity
Catalytic site (original residue number in PDB) R63 F68 Q71 N110 F121 L130 H134
Catalytic site (residue number reindexed from 1) R57 F62 Q65 N104 F115 L124 H128
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0005518 collagen binding
GO:0016018 cyclosporin A binding
GO:0051082 unfolded protein binding
GO:0070063 RNA polymerase binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0030593 neutrophil chemotaxis
GO:0040018 positive regulation of multicellular organism growth
GO:0044794 positive regulation by host of viral process
GO:0044829 positive regulation by host of viral genome replication
GO:0050821 protein stabilization
GO:0060348 bone development
GO:0061077 chaperone-mediated protein folding
GO:1901873 regulation of post-translational protein modification
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005790 smooth endoplasmic reticulum
GO:0005829 cytosol
GO:0005925 focal adhesion
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0034663 endoplasmic reticulum chaperone complex
GO:0042470 melanosome
GO:0043231 intracellular membrane-bounded organelle
GO:0048471 perinuclear region of cytoplasm
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1cyn, PDBe:1cyn, PDBj:1cyn
PDBsum1cyn
PubMed8197205
UniProtP23284|PPIB_HUMAN Peptidyl-prolyl cis-trans isomerase B (Gene Name=PPIB)

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