› 5dqy

X-ray diffraction
1.4Å resolution

A fully oxidized human thioredoxin

Released:
DOI: 10.2210/pdb5dqy/pdb
PDB entry 5dqy coloured by chain, front view.
PDB entry 5dqy coloured by chain, side view.
PDB entry 5dqy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of fully oxidized human thioredoxin.
Hwang J, Nguyen LT, Jeon YH, Lee CY, Kim MH
Biochem Biophys Res Commun 467 218-22 (2015)
PMID: 26453009

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-145348 (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
UniProt:
  • Canonical: P10599 (Residues: 1-105; Coverage: 100%)
Gene names: TRDX, TRX, TRX1, TXN
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand BEZ 1 x BEZ
Ligand CL 1 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: I222
Unit cell:
a: 53.204Å b: 61.231Å c: 64.839Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.209
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Redox regulation of tumor suppressor PTEN in cell signaling.
Zhang et al. (2020)
1 more

7 mentions without citation

Chemical Biology of H2S Signaling through Persulfidation.
Filipovic et al. (2018)
6 more