1JHN

Crystal Structure of the Lumenal Domain of Calnexin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.377 
  • R-Value Work: 0.327 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

Schrag, J.D.Bergeron, J.J.Li, Y.Borisova, S.Hahn, M.Thomas, D.Y.Cygler, M.

(2001) Mol Cell 8: 633-644

  • DOI: https://doi.org/10.1016/s1097-2765(01)00318-5
  • Primary Citation of Related Structures:  
    1JHN

  • PubMed Abstract: 

    The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the calnexin family of chaperones interacts with monoglucosylated glycoproteins.


  • Organizational Affiliation

    Biotechnology Research Institute, NRC, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada. joe@bri.nrc.ca


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
calnexin424Canis lupus familiarisMutation(s): 0 
UniProt
Find proteins for P24643 (Canis lupus familiaris)
Explore P24643 
Go to UniProtKB:  P24643
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24643
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CA
Query on CA

Download Ideal Coordinates CCD File 
B [auth A]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.377 
  • R-Value Work: 0.327 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.772α = 90
b = 85.772β = 90
c = 143.476γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-10-10
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance