Mercury in PDB 1g3z: Carbonic Anhydrase II (F131V)

All present enzymatic activity of Carbonic Anhydrase II (F131V):
4.2.1.1;

The structure of Carbonic Anhydrase II (F131V), PDB code: 1g3z was solved by C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.86
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.790, 41.830, 72.880, 90.00, 104.69, 90.00
R / Rfree (%)	18.2 / 23.4

The structure of Carbonic Anhydrase II (F131V) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Carbonic Anhydrase II (F131V) (pdb code 1g3z). 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 Carbonic Anhydrase II (F131V), PDB code: 1g3z:

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II (F131V)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II (F131V) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg263 b:33.6 occ:1.00 O A:VAL135 2.8 29.4 1.0 O A:GLN137 3.0 14.6 1.0 CB A:CYS206 3.1 14.4 1.0 C A:GLN137 3.2 16.9 1.0 N A:GLN137 3.3 18.0 1.0 C A:GLN136 3.4 21.6 1.0 O A:GLU205 3.6 13.3 1.0 CA A:CYS206 3.6 13.2 1.0 CA A:GLN137 3.7 18.9 1.0 C A:VAL135 3.8 22.9 1.0 O A:GLN136 3.8 20.7 1.0 C A:GLU205 3.8 11.6 1.0 N A:CYS206 3.9 11.6 1.0 N A:PRO138 3.9 15.8 1.0 CA A:GLN136 4.0 21.3 1.0 O A:HOH371 4.1 24.4 1.0 N A:GLN136 4.3 21.0 1.0 CA A:PRO138 4.4 15.0 1.0 SG A:CYS206 4.4 21.3 1.0 N A:GLU205 4.6 7.2 1.0 O A:HOH368 4.6 25.9 1.0 CA A:GLU205 4.8 8.6 1.0 CB A:LEU204 4.9 9.4 1.0 CA A:VAL135 4.9 19.4 1.0 O A:ALA134 5.0 17.9 1.0

C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson. Contribution of Fluorine to Protein-Ligand Affinity in the Binding of Fluoroaromatic Inhibitors to Carbonic Anhydrase II J.Am.Chem.Soc. V. 122 12125 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA002627N