› 1kng

X-ray diffraction
1.14Å resolution

Crystal structure of CcmG reducing oxidoreductase at 1.14 A

Released:
DOI: 10.2210/pdb1kng/pdb
PDB entry 1kng coloured by chain, front view.
PDB entry 1kng coloured by chain, side view.
PDB entry 1kng coloured by chain, top view.
Source organism: Bradyrhizobium japonicum
Primary publication:
Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment.
Edeling MA, Guddat LW, Fabianek RA, Thöny-Meyer L, Martin JL
Structure 10 973-9 (2002)
PMID: 12121652

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-151851 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein CycY Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 16.89 KDa
Source organism: Bradyrhizobium japonicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30960 (Residues: 39-194; Coverage: 99%)
Gene names: blr0471, ccmG, cycY
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1, null
Spacegroup: P212121
Unit cell:
a: 35.1Å b: 48.2Å c: 90.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
not available not available 0.151
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Protein disulfide isomerase: the structure of oxidative folding.
Gruber et al. (2006)
11 more

10 mentions without citation

Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.
Travaglini-Allocatelli C. (2013)
9 more