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UniProt Q00688

Peptidyl-prolyl cis-trans isomerase FKBP3 (Q00688)

Peptidyl-prolyl cis-trans isomerase FKBP3 (UniProt Q00688), EC 5.2.1.8: 10 experimental structures and 1 predicted model on GenesisL1, 3 ligands bound, 2 pockets. Binding sites, druggability and experiment against prediction…

UniProt
Q00688
Protein
Peptidyl-prolyl cis-trans isomerase FKBP3
EC
5.2.1.8
Experimental structures
10
Predicted models
1
Ligands
3
Pockets
2 · 1 record with a druggable one

Structures

11 records of Q00688 in the MolNFT archive: 10 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1PBKHomologous domain of human FKBP25x-ray diffractionA——
1PBKHomologous domain of human FKBP25x-ray diffractionA——
2KFVStructure of the amino-terminal domain of human FK506-binding protein 3 / Northeast Structural…solution nmrA——
2KFVStructure of the amino-terminal domain of human FK506-binding protein 3 / northeast structural…solution nmrA——
2MPHSolution Structure of human FK506 binding Protein 25solution nmrA——
2MPHSolution structure of human FK506 binding protein 25solution nmrA——
5D75Crystal structure of Human FKBD25 in complex with FK506x-ray diffractionAFK5, JEF1 (best 0.37)
5D75Crystal structure of human FKBD25 in complex with FK506x-ray diffractionA——
5GPGCo-crystal structure of the FK506 binding domain of human FKBP25, Rapamycin and the FRB domain of…x-ray diffractionARAP1 (best 0.78)
5GPGCo-crystal structure of the FK506 binding domain of human FKBP25, rapamycin and the frb domain of…x-ray diffractionA——
Q00688AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP3 (Q00688)predictedA——

Ligands

  • FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · in 1 record
  • JEF · O-(O-(2-aminopropyl)-O'-(2-methoxyethyl)polypropylene glycol 500) · in 1 record
  • RAP · Rapamycin immunosuppressant drug · in 1 record

Experiment against prediction

Elsewhere

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