1CYN

CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Work: 0.160 
  • R-Value Observed: 0.160 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

X-Ray Structure of a Cyclophilin B/Cyclosporin Complex: Comparison with Cyclophilin a and Delineation of its Calcineurin-Binding Domain.

Mikol, V.Kallen, J.Walkinshaw, M.D.

(1994) Proc Natl Acad Sci U S A 91: 5183

  • DOI: https://doi.org/10.1073/pnas.91.11.5183
  • Primary Citation of Related Structures:  
    1CYN

  • PubMed Abstract: 

    The crystal structure of a complex between recombinant human cyclophilin B (CypB) and a cyclosporin A (CsA) analog has been determined and refined at 1.85-A resolution to a crystallographic R factor of 16.0%. The overall structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. The network of the water-mediated contacts is also essentially conserved. The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are likely to modulate the differences in calcineurin inhibition between CypA and CypB.


  • Organizational Affiliation

    Preclinical Research, Sandoz AG, Basel, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B178Homo sapiensMutation(s): 0 
Gene Names: CYCLOPHILIN
EC: 5.2.1.8
UniProt & NIH Common Fund Data Resources
Find proteins for P23284 (Homo sapiens)
Explore P23284 
Go to UniProtKB:  P23284
PHAROS:  P23284
GTEx:  ENSG00000166794 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23284
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CYCLOSPORIN AB [auth C]11Tolypocladium inflatumMutation(s): 1 
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 [auth C]L-PEPTIDE LINKINGC4 H9 N O2ALA
BMT
Query on BMT
B [auth C]L-PEPTIDE LINKINGC10 H19 N O3THR
MLE
Query on MLE
B [auth C]L-PEPTIDE LINKINGC7 H15 N O2LEU
MVA
Query on MVA
B [auth C]L-PEPTIDE LINKINGC6 H13 N O2VAL
SAR
Query on SAR
B [auth C]PEPTIDE LINKINGC3 H7 N O2GLY
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Work: 0.160 
  • R-Value Observed: 0.160 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 37.46α = 90
b = 46.944β = 90
c = 115.442γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-01-29
    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: 2018-09-12
    Changes: Data collection, Other, Structure summary