› 4tw5

X-ray diffraction
2.37Å resolution

Structure Of the First Two Thioredoxin Domains of Saccharomyces cerevisiae Eps1p

Released:
DOI: 10.2210/pdb4tw5/pdb
PDB entry 4tw5 coloured by chain, front view.
PDB entry 4tw5 coloured by chain, side view.
PDB entry 4tw5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae JAY291
Primary publication:
The Eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino acid motifs but not their functional geometries.
Biran S, Gat Y, Fass D
PLoS One 9 e113431 (2014)
PMID: 25437863

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111710 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 272 amino acids
Theoretical weight: 31.32 KDa
Source organism: Saccharomyces cerevisiae JAY291
Expression system: Escherichia coli
UniProt:
  • Canonical: C7GJH6 (Residues: 28-295; Coverage: 40%)
Gene names: C1Q_00313, EPS1
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 40.026Å b: 133.031Å c: 124.406Å
α: 90° β: 92° γ: 90°
R-values:
R R work R free
0.215 0.212 0.272
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)
1 more

2 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
1 more