Mercury in PDB 2kt3: Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase

All present enzymatic activity of Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase:
1.16.1.1;

The binding sites of Mercury atom in the Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase (pdb code 2kt3). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase, PDB code: 2kt3:

Mercury binding site 1 out of 1 in the Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of Hg-Nmera, Hg(II) Complex of the N-Terminal Domain of TN501 Mercuric Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg70 b:0.0 occ:1.00 HB3 A:MET9 2.2 0.0 1.0 SG A:CYS14 2.3 0.0 1.0 SG A:CYS11 2.3 0.0 1.0 H A:CYS11 2.7 0.0 1.0 N A:CYS11 3.2 0.0 1.0 CB A:CYS11 3.2 0.0 1.0 HB2 A:CYS11 3.2 0.0 1.0 H A:CYS14 3.3 0.0 1.0 CB A:MET9 3.3 0.0 1.0 CA A:CYS11 3.5 0.0 1.0 O A:CYS11 3.5 0.0 1.0 C A:MET9 3.6 0.0 1.0 HB2 A:SER13 3.7 0.0 1.0 SD A:MET9 3.7 0.0 1.0 N A:THR10 3.8 0.0 1.0 C A:CYS11 3.8 0.0 1.0 CB A:CYS14 3.8 0.0 1.0 H A:THR10 3.8 0.0 1.0 HB2 A:CYS14 3.9 0.0 1.0 CA A:MET9 3.9 0.0 1.0 HB2 A:MET9 3.9 0.0 1.0 HA A:MET9 3.9 0.0 1.0 O A:MET9 4.0 0.0 1.0 C A:THR10 4.0 0.0 1.0 CG A:MET9 4.1 0.0 1.0 HB3 A:CYS11 4.2 0.0 1.0 N A:CYS14 4.2 0.0 1.0 CA A:THR10 4.5 0.0 1.0 H A:ALA15 4.5 0.0 1.0 HB3 A:CYS14 4.5 0.0 1.0 HA A:CYS11 4.6 0.0 1.0 H A:SER13 4.6 0.0 1.0 HG3 A:MET9 4.6 0.0 1.0 CA A:CYS14 4.7 0.0 1.0 CB A:SER13 4.8 0.0 1.0 N A:ASP12 4.8 0.0 1.0 HA A:THR10 4.9 0.0 1.0 N A:SER13 4.9 0.0 1.0 O A:THR10 4.9 0.0 1.0 HG2 A:MET9 4.9 0.0 1.0

R.Ledwidge, B.Hong, V.Dotsch, S.M.Miller. Nmera of TN501 Mercuric Ion Reductase: Structural Modulation of the Pka Values of the Metal Binding Cysteine Thiols. Biochemistry V. 49 8988 2010.
ISSN: ISSN 0006-2960
PubMed: 20828160
DOI: 10.1021/BI100537F