Structure of PDB 2rmc Chain C

Receptor sequence
>2rmcC (length=182) Species: 10090 (Mus musculus) [Search protein sequence]
KRGPSVTDKVFFDVRIGDKDVGRIVIGLFGNVVPKTVENFVALATGEKGY
GYKGSIFHRVIKDFMIQGGDFTARDGTGGMSIYGETFPDENFKLKHYGIG
WVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVLDGMTVVHSIELQA
TDGHDRPLTDCTIVNSGKIDVKTPFVVEVPDW
3D structure
PDB2rmc Crystal Structure of Murine Cyclophilin C Complexed with Immunosuppressive Drug Cyclosporin A
ChainC
Resolution1.64 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R89 F94 Q97 N136 F147 L156 H160
Catalytic site (residue number reindexed from 1) R59 F64 Q67 N106 F117 L126 H130
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 R89 F94 Q97 G106 A135 N136 A137 Q145 F147 W155 H160 R59 F64 Q67 G76 A105 N106 A107 Q115 F117 W125 H130
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:2rmc, PDBe:2rmc, PDBj:2rmc
PDBsum2rmc
PubMed8265636
UniProtP30412|PPIC_MOUSE Peptidyl-prolyl cis-trans isomerase C (Gene Name=Ppic)

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