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Ligands
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FK5 8-deethyl-8-[but-3-enyl]-ascomycin
Non-standard Residues
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Glycosylation
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Code : 3O5R   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : Complex of Fk506 with the Fk1 domain mutant A19T of FKBP51
Release Data : 2011-06-01
Compound :
mol_id molecule chains synonym
1 Peptidyl-prolyl cis-trans isomerase FKBP5 A PPIase FKBP5, FK506-binding protein 5, FKBP-5, Rotamase, 51 kDa FK506-binding protein, 51 kDa FKBP, FKBP-51, 54 kDa progesterone receptor-associated immunophilin, FKBP54, p54, FF1 antigen, HSP90-binding immunophilin, Androgen-regulated protein 6
ec: 5.2.1.8
mutation: A19T
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: AIG6, FKBP5, FKBP51
expression_system_strain: BL21(DE3) codon+ RIL
expression_system_vector_type: plasmid
expression_system_plasmid: pProEx-HtB
Authors : Bracher, A., Kozany, C., Thost, A.-K., Hausch, F.
Keywords : Fk-506 binding domain, Hsp90 cochaperone, immunophiline, peptidyl-prolyl isomerase, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 1.1000 Å )
Citation :

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.

Bracher, A.,Kozany, C.,Thost, A.K.  et al.
(2011)  Acta Crystallogr.,Sect.D  67 : 549 - 559

PubMed: 21636895
DOI: 10.1107/S0907444911013862

Chain : A
UniProt : Q13451 (FKBP5_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0) 5.2.1.8 PubMed:11350175
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