2ovi

X-ray diffraction
2.05Å resolution

Structure of the Heme Binding Protein ChuX

Released:
Source organism: Escherichia coli O157:H7
Primary publication:
Structure and heme binding properties of Escherichia coli O157:H7 ChuX.
Protein Sci. 18 825-38 (2009)
PMID: 19319934

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme utilization carrier protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 164 amino acids
Theoretical weight: 18.35 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8X5N5 (Residues: 1-164; Coverage: 100%)
Gene name: ECs_4384
Sequence domains: Haem utilisation ChuX/HutX
Structure domains: HemS/ChuS/ChuX like domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C, NSLS BEAMLINE X12C
Spacegroup: P41
Unit cell:
a: 76.56Å b: 76.56Å c: 140.864Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.25
Expression system: Escherichia coli BL21(DE3)