› 1auc

X-ray diffraction
2.1Å resolution

HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)

Released:
DOI: 10.2210/pdb1auc/pdb
PDB entry 1auc coloured by chain, front view.
PDB entry 1auc coloured by chain, side view.
PDB entry 1auc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant.
Andersen JF, Sanders DA, Gasdaska JR, Weichsel A, Powis G, Montfort WR
Biochemistry 36 13979-88 (1997)
PMID: 9369469

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: 11.75 KDa
Source organism: Homo sapiens
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: 67.75Å b: 26.29Å c: 51.62Å
α: 90° β: 95.14° γ: 90°
R-values:
R R work R free
0.19 0.19 0.27

Quick links

Citations

9 review citations

The role of the redox protein thioredoxin in cell growth and cancer.
Powis et al. (2000)
8 more

4 mentions without citation

Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.
Meng et al. (2011)
3 more