› 2hls

X-ray diffraction
1.93Å resolution

The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1

Released:
DOI: 10.2210/pdb2hls/pdb
PDB entry 2hls coloured by chain, front view.
PDB entry 2hls coloured by chain, side view.
PDB entry 2hls coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics.
D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
J Mol Biol 362 743-52 (2006)
PMID: 16934838

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-195483 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-like fold domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 27.36 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YDZ4 (Residues: 1-243; Coverage: 100%)
Gene name: APE_0775
Sequence domains: Thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: I222
Unit cell:
a: 90.625Å b: 101.424Å c: 128.927Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.209
Expression system: Escherichia coli

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Citations

7 review citations

Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.
Roos et al. (2013)
6 more

1 mention without citation

Multidimensional Honeycomb-like DNA Nanostructures Made of C-Motifs.
Tandon et al. (2023)