› 3apq

X-ray diffraction
1.84Å resolution

Crystal structure of J-Trx1 fragment of ERdj5

Released:
DOI: 10.2210/pdb3apq/pdb
PDB entry 3apq coloured by chain, front view.
PDB entry 3apq coloured by chain, side view.
PDB entry 3apq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5.
Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K
Mol Cell 41 432-44 (2011)
PMID: 21329881

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190098 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DnaJ homolog subfamily C member 10 Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 24.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9DC23 (Residues: 34-242; Coverage: 28%)
Gene names: Dnajc10, Erdj5, Jpdi
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 54.008Å b: 61.179Å c: 62.912Å
α: 90° β: 106.34° γ: 90°
R-values:
R R work R free
0.173 0.17 0.23
Expression system: Escherichia coli

Quick links

Citations

40 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
39 more

1 mention without citation

C-terminal Redox Domain of Arabidopsis APR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function.
Chen et al. (2019)