› 2kt3

Solution NMR

Structure of Hg-NmerA, Hg(II) complex of the N-terminal domain of Tn501 Mercuric Reductase

Released:
DOI: 10.2210/pdb2kt3/pdb
PDB entry 2kt3 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kt3 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kt3 coloured by chain, ensemble of 20 models, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols.
Ledwidge R, Hong B, Dötsch V, Miller SM
Biochemistry 49 8988-98 (2010)
PMID: 20828160

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132463 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mercuric reductase Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 6.92 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P00392 (Residues: 1-69; Coverage: 12%)
Gene name: merA
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 83%
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli K-12

Quick links

Citations

2 review citations

Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.
Roos et al. (2013)
1 more