› 1aiu

X-ray diffraction
2Å resolution

HUMAN THIOREDOXIN (D60N MUTANT, REDUCED FORM)

Released:
DOI: 10.2210/pdb1aiu/pdb
PDB entry 1aiu coloured by chain, front view.
PDB entry 1aiu coloured by chain, side view.
PDB entry 1aiu 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
Expression system: Escherichia coli BL21(DE3)
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: 68.36Å b: 26.76Å c: 52.18Å
α: 90° β: 95.02° γ: 90°
R-values:
R R work R free
0.179 0.179 0.24
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

13 mentions without citation

Anticancer activity of metal complexes: involvement of redox processes.
Jungwirth et al. (2011)
12 more