2hxr

X-ray diffraction
2.05Å resolution

Structure of the ligand binding domain of E. coli CynR, a transcriptional regulator controlling cyanate metabolism

Released:
Source organism: Escherichia coli K-12
Entry authors: Singer AU, Cuff ME, Evdokimova E, Kagan O, Joachimiak A, Edwards AM, Savchenko A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-150929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH-type transcriptional regulator CynR Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 26.41 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27111 (Residues: 63-299; Coverage: 79%)
Gene names: JW5894, b0338, cynR
Sequence domains: LysR substrate binding domain
Structure domains: D-Maltodextrin-Binding Protein; domain 2

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 87.913Å b: 98.555Å c: 62.236Å
α: 90° β: 104.35° γ: 90°
R-values:
R R work R free
0.241 0.239 0.256
Expression system: Escherichia coli BL21(DE3)