› 5u88

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
An alkylmercury + H(+) = an alkane + Hg(2+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkylmercury lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 23.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P77072 (Residues: 1-212; Coverage: 100%)
Gene name: merB
Sequence domains:
Structure domains: Beta-Lactamase

Ligands and Environments

2 bound ligands:
Ligand ZN9 2 x ZN9
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 38.467Å b: 88.789Å c: 54.734Å
α: 90° β: 97.87° γ: 90°
R-values:
R R work R free
0.178 0.176 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Genetic and Physiological Adaptations of Marine Bacterium Pseudomonas stutzeri 273 to Mercury Stress.
Zheng et al. (2018)
1 more

1 mention without citation

Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase MerB Provide New Insights into Its Mechanism of Carbon-Metal Bond Cleavage.
Wahba et al. (2017)