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PDBsum entry 2haq

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protein links
Isomerase PDB id
2haq
Jmol
Contents
Protein chain
166 a.a. *
Waters ×102
* Residue conservation analysis
PDB id:
2haq
Name: Isomerase
Title: Crystal structure of cyclophilin a from leishmania donovani
Structure: Cyclophilin. Chain: a. Engineered: yes
Source: Leishmania donovani. Organism_taxid: 5661. Gene: cyp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.97Å     R-factor:   0.178     R-free:   0.197
Authors: V.Venugopal,B.Sen,A.K.Datta,R.Banerjee.
Key ref:
V.Venugopal et al. (2007). Structure of cyclophilin from Leishmania donovani at 1.97 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 60-64. PubMed id: 17277440 DOI: 10.1107/S1744309106056351
Date:
13-Jun-06     Release date:   20-Jun-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9U9R3  (Q9U9R3_LEIDO) -  Peptidyl-prolyl cis-trans isomerase
Seq:
Struc:
187 a.a.
166 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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   2 terms 
  Biochemical function     peptidyl-prolyl cis-trans isomerase activity     1 term  

 

 
    Added reference    
 
 
DOI no: 10.1107/S1744309106056351 Acta Crystallogr Sect F Struct Biol Cryst Commun 63:60-64 (2007)
PubMed id: 17277440  
 
 
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.
V.Venugopal, B.Sen, A.K.Datta, R.Banerjee.
 
  ABSTRACT  
 
The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail.
 
  Selected figure(s)  
 
Figure 2.
Electron density contoured at the 2.5[sigma] level for residues Val29 --Val33 of LdCyp from a 2F [o] [minus sign] F [c] map. This figure and Figs. 3 --5 were generated using MOLSCRIPT/BOBSCRIPT (Kraulis, 1991[triangle]; Esnouf, 1999[triangle]) and RASTER3D (Merritt & Bacon, 1997[triangle]). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 February 1; 63(Pt 2): 60–64. Published online 2007 January 17. doi: 10.1107/S1744309106056351. Copyright [copyright] International Union of Crystallography 2007
Figure 4.
Wat31 (shown in red) bridging helix H3 and [beta]-strand B2. Hydrogen bonds are shown as dashed lines. Residues Leu40 from B2 and Arg163 from H3 are indicated. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 February 1; 63(Pt 2): 60–64. Published online 2007 January 17. doi: 10.1107/S1744309106056351. Copyright [copyright] International Union of Crystallography 2007
 
  The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2007, 63, 60-64) copyright 2007.  
  Figures were selected by an automated process.