You can find more information about peptidyl-prolyl cis-trans isomerase fkbp using the following links:

PFID

PFID Old

Formal Annotation

PlasmoDB

TDR Targets

Subcellular Localization

Affecting Drugs

Drug Name

PubMed Articles (year of publication)

PF3D7_1247400

PFL2275c

peptidyl-prolyl cis-trans isomerase fkbp

PlasmoDB

TDR

(1S,5S,6R)-10-((3,5-Dichlorophenyl)sulfonyl)-5- ethyl-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one.	Structural insights into Plasmodium PPIases
(R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl (S)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate	Targeted Covalent Inhibition of Plasmodium FK506 Binding Protein 35
13-dM(Me)-18-OH-Fk520	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
13-dM(Me)-Fk520	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
18-OH-FK520	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
2-bromo-3-methyl-1,4-dimethoxy-9,10-anthraquinone	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
4'-sub-1,2,3,4-tetrahydrorapamycin	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Ascomycin	The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity
Carbocyclic thymidine	Targeting FK506 binding proteins to fight malarial and bacterial infections: current advances and future perspectives
cyclosporin A	Immunophilin-protein interactions in Plasmodium falciparum
Cyclosporin a	A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities
D44	Structural insights into Plasmodium PPIases
Desmethoxyrapamycin	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Desmethylrapamycin	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Fk506	Expression, purification, and molecular characterization of Plasmodium falciparum FK506-binding protein 35 (PfFKBP35) Crystal structure of the FK506 binding domain of Plasmodium falciparum FKBP35 in complex with FK506 Molecular docking study of macrocycles as Fk506-binding protein inhibitors 1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35
Fk506	The antimalarial action of FK506 and rapamycin: evidence for a direct effect on FK506-binding protein PfFKBP35 Structural insights into Plasmodium PPIases Immunophilin-protein interactions in Plasmodium falciparum Molecular docking study of macrocycles as Fk506-binding protein inhibitors A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities
Fk520	Molecular docking study of macrocycles as Fk506-binding protein inhibitors Antimalarial effects of macrolactones related to FK520 (ascomycin) are independent of the immunosuppressive properties of the compounds
Ils-920	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Imidazopyrazines	Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity
immunomycin derivative	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Kdu691	Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity
N-(2-ethyl-phenyl)-2-(3h-imidazao [4, 5-b] pyridin-2-yl-sulfanyl)-acetamide	Small molecule Plasmodium FKBP35 inhibitor as a potential antimalaria agent
Prolylrapamycin	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Quinolone	A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities
rapamycin	The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity The antimalarial action of FK506 and rapamycin: evidence for a direct effect on FK506-binding protein PfFKBP35 Structural insights into Plasmodium PPIases Two crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Suggested target	Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity
Tacrolimus	Computational insights into the suicide inhibition of Plasmodium falciparum Fk506-binding protein 35
Way-179639	Molecular docking study of macrocycles as Fk506-binding protein inhibitors
Wye-592	Molecular docking study of macrocycles as Fk506-binding protein inhibitors

Expasy - NiceZime View
Brenda - The Comprehensive Enzyme Information System