› 1zk7

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
Hg + NADP(+) + H(+) = Hg(2+) + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mercuric reductase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 49.23 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00392 (Residues: 96-561; Coverage: 83%)
Gene name: merA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
Ligand SO4 3 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43212
Unit cell:
a: 86.788Å b: 86.788Å c: 136.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Toxicity of Glutathione-Binding Metals: A Review of Targets and Mechanisms.
Rubino FM. (2015)
1 more

14 mentions without citation

Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality.
Cooley et al. (2010)
13 more