› 1jhn

X-ray diffraction
2.9Å resolution

Crystal Structure of the Lumenal Domain of Calnexin

Released:
DOI: 10.2210/pdb1jhn/pdb
PDB entry 1jhn coloured by chain, front view.
PDB entry 1jhn coloured by chain, side view.
PDB entry 1jhn coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M
Mol Cell 8 633-44 (2001)
PMID: 11583625

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150264 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calnexin Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 48.29 KDa
Source organism: Canis lupus familiaris
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P24643 (Residues: 45-468; Coverage: 74%)
Gene name: CANX
Sequence domains: Calreticulin family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P43212
Unit cell:
a: 85.772Å b: 85.772Å c: 143.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.327 0.327 0.377
Expression system: Spodoptera frugiperda

Quick links

Citations

55 review citations

Quality control in the endoplasmic reticulum.
Ellgaard et al. (2003)
54 more

30 mentions without citation

N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control.
Moremen et al. (2006)
29 more