2WFJ

Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in complex with cyclosporin A.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.75 Å
  • R-Value Free: 0.129 
  • R-Value Observed: 0.111 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The Thermodynamic Influence of Trapped Water Molecules on a Protein-Ligand Interaction.

Stegmann, C.M.Seeliger, D.Sheldrick, G.M.De Groot, B.L.Wahl, M.C.

(2009) Angew Chem Int Ed Engl 48: 5207

  • DOI: https://doi.org/10.1002/anie.200900481
  • Primary Citation of Related Structures:  
    2WFI, 2WFJ

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Research Group X-ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G179Homo sapiensMutation(s): 0 
EC: 5.2.1.8
UniProt & NIH Common Fund Data Resources
Find proteins for Q13427 (Homo sapiens)
Explore Q13427 
Go to UniProtKB:  Q13427
PHAROS:  Q13427
GTEx:  ENSG00000138398 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13427
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CYCLOSPORIN A11Tolypocladium inflatumMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  5 Unique
IDChains TypeFormula2D DiagramParent
ABA
Query on ABA
B
L-PEPTIDE LINKINGC4 H9 N O2ALA
BMT
Query on BMT
B
L-PEPTIDE LINKINGC10 H19 N O3THR
MLE
Query on MLE
B
L-PEPTIDE LINKINGC7 H15 N O2LEU
MVA
Query on MVA
B
L-PEPTIDE LINKINGC6 H13 N O2VAL
SAR
Query on SAR
B
PEPTIDE LINKINGC3 H7 N O2GLY
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.75 Å
  • R-Value Free: 0.129 
  • R-Value Observed: 0.111 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.319α = 90
b = 64.913β = 90
c = 69.285γ = 90
Software Package:
Software NamePurpose
SHELXL-97refinement
XDSdata reduction
XDSdata scaling
SHELXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-06-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Atomic model, Database references, Derived calculations, Structure summary, Version format compliance
  • Version 1.2: 2011-11-23
    Changes: Database references
  • Version 1.3: 2012-11-30
    Changes: Other
  • Version 1.4: 2019-05-22
    Changes: Data collection, Derived calculations, Other, Refinement description