› 5i0x

X-ray diffraction
1.5Å resolution

COPPER-BOUND M90I VARIANT OF UROPATHOGENIC ESCHERICHIA COLI STRAIN F11 FETP

Released:
DOI: 10.2210/pdb5i0x/pdb
PDB 5i0x coloured by chain and viewed from the front.
PDB 5i0x coloured by chain and viewed from the side.
PDB 5i0x coloured by chain and viewed from the top.
Source organism: Escherichia coli F11
Primary publication:
A copper site is required for iron transport by the periplasmic proteins P19 and FetP.
Chan ACK, Lin H, Koch D, Grass G, Nies DH, Murphy MEP
Metallomics 12 1530-1541 (2020)
PMID: 32780051

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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: 17.64 KDa
Source organism: Escherichia coli F11
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1S4NYE6 (Residues: 3-153; Coverage: 94%)
Gene name: EcF11_1994
Sequence domains: Fe2+ transport protein
Structure domains: Periplasmic metal-binding protein Tp34-type

Ligands and Environments

1 bound ligand:
Ligand CU 3 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 49.155Å b: 51.612Å c: 66.136Å
α: 90° β: 93.3° γ: 90°
R-values:
R R work R free
0.178 0.176 0.208
Expression system: Escherichia coli BL21(DE3)

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