3nrq

X-ray diffraction
1.7Å resolution

Crystal structure of copper-reconstituted FetP from uropathogenic Escherichia coli strain F11

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-163823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic protein-probably involved in high-affinity Fe2+ transport Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.66 KDa
Source organism: Escherichia coli F11
Expression system: Escherichia coli BL21(DE3)
Structure domains: Periplasmic metal-binding protein Tp34-type

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 38.41Å b: 51.97Å c: 146.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.235
Expression system: Escherichia coli BL21(DE3)