› 1erw

X-ray diffraction
1.8Å resolution

HUMAN THIOREDOXIN DOUBLE MUTANT WITH CYS 32 REPLACED BY SER AND CYS 35 REPLACED BY SER

Released:
DOI: 10.2210/pdb1erw/pdb
PDB entry 1erw coloured by chain, front view.
PDB entry 1erw coloured by chain, side view.
PDB entry 1erw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.
Weichsel A, Gasdaska JR, Powis G, Montfort WR
Structure 4 735-51 (1996)
PMID: 8805557

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10599 (Residues: 1-105; Coverage: 100%)
Gene names: TRDX, TRX, TRX1, TXN
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 67.77Å b: 26.38Å c: 51.64Å
α: 90° β: 95.08° γ: 90°
R-values:
R R work R free
0.21 0.21 0.26
Expression system: Escherichia coli

Quick links

Citations

40 review citations

Physiological functions of thioredoxin and thioredoxin reductase.
Arnér et al. (2000)
39 more

1 mention without citation

Stereochemical configuration of 4-hydroxy-2-nonenal-cysteine adducts and their stereoselective formation in a redox-regulated protein.
Wakita et al. (2009)