› 3uvt

X-ray diffraction
2Å resolution

Crystal structure of the third catalytic domain of ERp46

Released:
DOI: 10.2210/pdb3uvt/pdb
PDB entry 3uvt coloured by chain, front view.
PDB entry 3uvt coloured by chain, side view.
PDB entry 3uvt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the third catalytic domain of the protein disulfide isomerase ERp46.
Gulerez IE, Kozlov G, Rosenauer A, Gehring K
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 378-81 (2012)
PMID: 22505402

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185480 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein 5 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 111 amino acids
Theoretical weight: 12.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NBS9 (Residues: 323-428; Coverage: 27%)
Gene names: TLP46, TXNDC5, UNQ364/PRO700
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 68.106Å b: 61.886Å c: 71.002Å
α: 90° β: 106.37° γ: 90°
R-values:
R R work R free
0.207 0.204 0.245
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration.
Halloran et al. (2013)
3 more

5 mentions without citation

Functions and mechanisms of protein disulfide isomerase family in cancer emergence.
Rahman et al. (2022)
4 more