1C5F

CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.47 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.201 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

Crystal Structure of the Complex of Brugia Malayi Cyclophilin and Cyclosporin A.

Ellis, P.J.Carlow, C.K.Ma, D.Kuhn, P.

(2000) Biochemistry 39: 592

  • DOI: https://doi.org/10.1021/bi991730q
  • Primary Citation of Related Structures:  
    1C5F

  • PubMed Abstract: 

    The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 A in this region.


  • Organizational Affiliation

    Stanford Synchrotron Radiation Laboratory, SLAC, P.O. Box 4249, Bin 69, Stanford University, Stanford, California 94309, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 1
A, C, E, G, I
A, C, E, G, I, K, M, O
177Brugia malayiMutation(s): 0 
Gene Names: BMCYP-1
EC: 5.2.1.8
UniProt
Find proteins for Q27450 (Brugia malayi)
Explore Q27450 
Go to UniProtKB:  Q27450
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ27450
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CYCLOSPORIN A
B, D, F, H, J
B, D, F, H, J, L, N, P
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
B, D, F, H, J
B, D, F, H, J, L, N, P
L-PEPTIDE LINKINGC4 H9 N O2ALA
BMT
Query on BMT
B, D, F, H, J
B, D, F, H, J, L, N, P
L-PEPTIDE LINKINGC10 H19 N O3THR
MLE
Query on MLE
B, D, F, H, J
B, D, F, H, J, L, N, P
L-PEPTIDE LINKINGC7 H15 N O2LEU
MVA
Query on MVA
B, D, F, H, J
B, D, F, H, J, L, N, P
L-PEPTIDE LINKINGC6 H13 N O2VAL
SAR
Query on SAR
B, D, F, H, J
B, D, F, H, J, L, N, P
PEPTIDE LINKINGC3 H7 N O2GLY
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.47 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.201 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62α = 90
b = 100.16β = 93.75
c = 133.92γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
MAR345data collection
MOSFLMdata reduction
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-12-03
    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: 2017-10-04
    Changes: Advisory, Refinement description
  • Version 1.6: 2023-12-27
    Changes: Advisory, Data collection, Database references, Derived calculations