Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
FK5 8-deethyl-8-[but-3-enyl]-ascomycin
Non-standard Residues
Code Name Show
MSE Selenomethionine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1Q6I   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : Crystal structure of a truncated form of FkpA from Escherichia coli, in complex with immunosuppressant FK506
Release Data : 2004-01-13
Compound :
mol_id molecule chains synonym
1 FKBP-type peptidyl-prolyl cis-trans isomerase fkpA A,B PPiase, Rotamase
ec: 5.2.1.8
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
gene: FKPA OR B3347
expression_system_strain: MC4100 derivative
expression_system_vector_type: plasmid
expression_system_plasmid: pTfkpDCT
Authors : Saul, F.A., Arie, J.-P., Vulliez-le Normand, B., Kahn, R., Betton, J.-M., Bentley, G.A.
Keywords : chaperone, peptidyl-prolyl isomerase, heat shock protein, FKBP family, immunosuppressant FK506, ascomycin, isomerase
Exp. method : X-RAY DIFFRACTION ( 2.25 Å )
Citation :

Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.

Saul, F.A.,Arie, J.P.,Vulliez-le Normand, B.  et al.
(2004)  J.Mol.Biol.  335 : 595 - 608

PubMed: 14672666
DOI: 10.1016/j.jmb.2003.10.056

Chain : A, B
UniProt : P45523 (FKBA_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0) 5.2.1.8 -
-