› 2c0e

X-ray diffraction
2.35Å resolution

Structure of PDI-related Chaperone, Wind with his-tag on C-terminus.

Released:
DOI: 10.2210/pdb2c0e/pdb
PDB entry 2c0e coloured by chain, front view.
PDB entry 2c0e coloured by chain, side view.
PDB entry 2c0e coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural elucidation of the PDI-related chaperone Wind with the help of mutants.
Sevvana M, Biadene M, Ma Q, Guo C, Söling HD, Sheldrick GM, Ferrari DM
Acta Crystallogr D Biol Crystallogr 62 589-94 (2006)
PMID: 16699185

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein windbeutel Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 28.55 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: O44342 (Residues: 21-257; Coverage: 100%)
Gene names: CG7225, wbl, wind
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2
Unit cell:
a: 107.782Å b: 50.368Å c: 98.675Å
α: 90° β: 112.19° γ: 90°
R-values:
R R work R free
0.23 0.226 0.293
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.
Roversi et al. (2017)
2 more