› 3d8x

X-ray diffraction
2.8Å resolution

Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1

Released:
DOI: 10.2210/pdb3d8x/pdb
PDB entry 3d8x coloured by chain, front view.
PDB entry 3d8x coloured by chain, side view.
PDB entry 3d8x coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin.
Zhang Z, Bao R, Zhang Y, Yu J, Zhou CZ, Chen Y
Biochim Biophys Acta 1794 124-8 (2009)
PMID: 18930846

Function and Biology Details

Reaction catalysed: 
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin reductase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 35.16 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P29509 (Residues: 2-319; Coverage: 100%)
Gene names: D9476.5, TRR1, YDR353W
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NDP 1 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 54.229Å b: 125.004Å c: 60.967Å
α: 90° β: 114.16° γ: 90°
R-values:
R R work R free
0.226 0.226 0.234
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Repurposing Auranofin, Ebselen, and PX-12 as Antimicrobial Agents Targeting the Thioredoxin System.
May et al. (2018)
9 other articles

2 mentions without citation

The role of structural pleiotropy and regulatory evolution in the retention of heteromers of paralogs.
Marchant et al. (2019)
1 more