1XQ7

Cyclophilin from Trypanosoma cruzi bound to cyclosporin A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.169 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Cyclophilin from Trypanosoma Cruzi Bound to Cyclosporin A

Caruthers, J.M.Hol, W.G.J.Structural Genomics of Pathogenic Protozoa Consortium

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
A, B, C
166Trypanosoma cruziMutation(s): 0 
EC: 5.2.1.8
UniProt
Find proteins for Q4DPB9 (Trypanosoma cruzi (strain CL Brener))
Explore Q4DPB9 
Go to UniProtKB:  Q4DPB9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4DPB9
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CYCLOSPORIN A
D, E, F
11Tolypocladium 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
D, E, F
L-PEPTIDE LINKINGC4 H9 N O2ALA
BMT
Query on BMT
D, E, F
L-PEPTIDE LINKINGC10 H19 N O3THR
MLE
Query on MLE
D, E, F
L-PEPTIDE LINKINGC7 H15 N O2LEU
MVA
Query on MVA
D, E, F
L-PEPTIDE LINKINGC6 H13 N O2VAL
SAR
Query on SAR
D, E, F
PEPTIDE LINKINGC3 H7 N O2GLY
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.169 
  • R-Value Observed: 0.172 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.269α = 110.49
b = 57.059β = 108.21
c = 58.807γ = 105.4
Software Package:
Software NamePurpose
EPMRphasing
REFMACrefinement
ELVESdata reduction
ELVESdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-12-21
    Type: Initial release
  • Version 1.1: 2011-06-14
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2011-07-27
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Structure summary
  • Version 1.4: 2012-12-12
    Changes: Other
  • Version 1.5: 2018-01-31
    Changes: Database references
  • Version 1.6: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.7: 2023-11-15
    Changes: Data collection, Derived calculations