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BioLiP

Structure of PDB 1c5f Chain C

Receptor sequence
>1c5fC (length=177) Species: 6279 (Brugia malayi) [Search protein sequence]
MSKKDRRRVFLDVTIDGNLAGRIVMELYNDIAPRTCNNFLMLCTGMAGTG
KISGKPLHYKGSTFHRVIKNFMIQGGDFTKGDGTGGESIYGGMFDDEEFV
MKHDEPFVVSMANKGPNTNGSQFFITTTPAPHLNNIHVVFGKVVSGQEVV
TKIEYLKTNSKNRPLADVVILNCGELV
3D structure
PDB1c5f Crystal Structure of the Complex of Brugia Malayi Cyclophilin and Cyclosporin A.
ChainC
Resolution2.47 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R66 F71 Q74 N113 F124 L133 H137
Catalytic site (residue number reindexed from 1) R66 F71 Q74 N113 F124 L133 H137
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide C R66 F71 Q74 G83 A112 N113 K114 Q122 F124 H132 H137 R66 F71 Q74 G83 A112 N113 K114 Q122 F124 H132 H137
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:1c5f, PDBe:1c5f, PDBj:1c5f
PDBsum1c5f
PubMed10642184
UniProtQ27450|CYP1_BRUMA Peptidyl-prolyl cis-trans isomerase 1 (Gene Name=CYP-1)

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