PDBsum entry 2wfi

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protein metals links
Isomerase PDB id
Protein chain
172 a.a. *
_MG ×2
Waters ×432
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Atomic resolution crystal structure of the ppiase domain of human cyclophilin g
Structure: Peptidyl-prolyl cis-trans isomerase g. Chain: a. Fragment: ppiase domain, residues 1-177. Synonym: cyclophilin g, clk-associating rs-cyclophilin, casp10, peptidyl-prolyl isomerase g, ppiase g, rotamase g, cars-cyclophilin, cars-cyp, sr-cyclophilin, sr-cyp, srcyp. Engineered: yes. Other_details: cys63 oxidized to cysteine sulfonic acid
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
0.75Å     R-factor:   0.107     R-free:   0.124
Authors: C.M.Stegmann,G.M.Sheldrick,M.C.Wahl
Key ref: C.M.Stegmann et al. (2009). The thermodynamic influence of trapped water molecules on a protein-ligand interaction. Angew Chem Int Ed Engl, 48, 5207-5210. PubMed id: 19499554
06-Apr-09     Release date:   16-Jun-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q13427  (PPIG_HUMAN) -  Peptidyl-prolyl cis-trans isomerase G
754 a.a.
172 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - 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    
Angew Chem Int Ed Engl 48:5207-5210 (2009)
PubMed id: 19499554  
The thermodynamic influence of trapped water molecules on a protein-ligand interaction.
C.M.Stegmann, D.Seeliger, G.M.Sheldrick, Groot, M.C.Wahl.
Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20368803 C.M.Stegmann, R.Lührmann, and M.C.Wahl (2010).
The crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP protein.
  PLoS One, 5, e10013.
PDB code: 2x7k
19923714 V.Venugopal, A.K.Datta, D.Bhattacharyya, D.Dasgupta, and R.Banerjee (2009).
Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data.
  Acta Crystallogr D Biol Crystallogr, 65, 1187-1195.
PDB code: 3eov
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