› 1a8l

X-ray diffraction
1.9Å resolution

PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS

Released:
DOI: 10.2210/pdb1a8l/pdb
PDB entry 1a8l coloured by chain, front view.
PDB entry 1a8l coloured by chain, side view.
PDB entry 1a8l coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units.
Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S, Ladenstein R
Nat Struct Biol 5 602-11 (1998)
PMID: 9665175

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-like fold domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.81 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q51760 (Residues: 1-226; Coverage: 100%)
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P6522
Unit cell:
a: 110.291Å b: 110.291Å c: 68.514Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.217
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads.
Karshikoff et al. (2001)
21 more

4 mentions without citation

The genomics of disulfide bonding and protein stabilization in thermophiles.
Beeby et al. (2005)
3 more