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PDBsum entry 3o5r

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protein ligands links
Isomerase PDB id
3o5r
Jmol
Contents
Protein chain
128 a.a.
Ligands
FK5
Waters ×298
PDB id:
3o5r
Name: Isomerase
Title: Complex of fk506 with the fk1 domain mutant a19t of fkbp51
Structure: Peptidyl-prolyl cis-trans isomerase fkbp5. Chain: a. Synonym: ppiase fkbp5, fk506-binding protein 5, fkbp-5, rot kda fk506-binding protein, 51 kda fkbp, fkbp-51, 54 kda pro receptor-associated immunophilin, fkbp54, p54, ff1 antigen, binding immunophilin, androgen-regulated protein 6. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aig6, fkbp5, fkbp51. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.10Å     R-factor:   0.124     R-free:   0.157
Authors: A.Bracher,C.Kozany,A.-K.Thost,F.Hausch
Key ref: A.Bracher et al. (2011). Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90. Acta Crystallogr D Biol Crystallogr, 67, 549-559. PubMed id: 21636895 DOI: 10.1107/S0907444911013862
Date:
28-Jul-10     Release date:   01-Jun-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13451  (FKBP5_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP5
Seq:
Struc:
457 a.a.
128 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 

 

 
    Added reference    
 
 
DOI no: 10.1107/S0907444911013862 Acta Crystallogr D Biol Crystallogr 67:549-559 (2011)
PubMed id: 21636895  
 
 
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.
A.Bracher, C.Kozany, A.K.Thost, F.Hausch.
 
  ABSTRACT  
 
No abstract given.