› 5co3

X-ray diffraction
1.65Å resolution

Crystal structure of a novel disulfide oxidoreductase from Deinococcus radiodurans crystallized in presence of DTT

Released:
DOI: 10.2210/pdb5co3/pdb
PDB entry 5co3 coloured by chain, front view.
PDB entry 5co3 coloured by chain, side view.
PDB entry 5co3 coloured by chain, top view.
Source organism: Deinococcus radiodurans R1
Primary publication:
drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.
Bihani SC, Panicker L, Rajpurohit YS, Misra HS, Kumar V
Antioxid Redox Signal 28 296-310 (2018)
PMID: 28899103

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DSBA-like thioredoxin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 28.49 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RWK7 (Residues: 1-252; Coverage: 100%)
Gene name: DR_0659
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RRCAT INDUS-2 BEAMLINE PX-BL21
Unit cell:
a: 47.729Å b: 63.52Å c: 86.247Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.
Lim et al. (2019)
1 more

1 mention without citation

Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans.
Chen et al. (2020)