› 1quw

Solution NMR

SOLUTION STRUCTURE OF THE THIOREDOXIN FROM BACILLUS ACIDOCALDARIUS

Released:
DOI: 10.2210/pdb1quw/pdb
PDB entry 1quw coloured by chain, ensemble of 20 models, front view.
PDB entry 1quw coloured by chain, ensemble of 20 models, side view.
PDB entry 1quw coloured by chain, ensemble of 20 models, top view.
Source organism: Alicyclobacillus acidocaldarius
Primary publication:
NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.
Nicastro G, De Chiara C, Pedone E, Tatò M, Rossi M, Bartolucci S
Eur J Biochem 267 403-13 (2000)
PMID: 10632710

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.59 KDa
Source organism: Alicyclobacillus acidocaldarius
Expression system: Escherichia coli
UniProt:
  • Canonical: P80579 (Residues: 1-105; Coverage: 100%)
Gene name: trxA
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS AND RESTRAINED ENERGY MINIMISATION
Expression system: Escherichia coli

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Citations

1 review citation

The machinery for oxidative protein folding in thermophiles.
Pedone et al. (2008)
10 other articles

1 mention without citation

An optimal distance cutoff for contact-based Protein Structure Networks using side-chain centers of mass.
Salamanca Viloria et al. (2017)