› 5aq6

X-ray diffraction
1.79Å resolution

Structure of E. coli ZinT at 1.79 Angstrom

Released:
DOI: 10.2210/pdb5aq6/pdb
PDB entry 5aq6 coloured by chain, front view.
PDB entry 5aq6 coloured by chain, side view.
PDB entry 5aq6 coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism.
Colaço HG, Santo PE, Matias PM, Bandeiras TM, Vicente JB
Metallomics 8 327-36 (2016)
PMID: 26758285

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metal-binding protein ZinT Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 22.4 KDa
Source organism: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P76344 (Residues: 24-216; Coverage: 100%)
Gene names: JW1956, b1973, yodA, zinT
Sequence domains: ZinT (YodA) periplasmic lipocalin-like zinc-recruitment
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 62.01Å b: 62.01Å c: 149.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.208

Quick links

Citations

1 review citation

How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores.
Bellotti et al. (2021)
3 other articles