Mercury in PDB 6gm9: Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide, PDB code: 6gm9 was solved by S.Gloeckner, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.79 / 1.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.365, 41.472, 72.273, 90.00, 104.66, 90.00
R / Rfree (%)	10.3 / 11.8

The structure of Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide (pdb code 6gm9). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide, PDB code: 6gm9:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg302 b:7.6 occ:0.16 HG A:MBO307 1.3 9.7 0.8 SG A:CYS206 1.3 8.3 0.8 HB3 A:CYS206 2.0 7.5 0.2 SG A:CYS206 2.5 6.7 0.2 O A:HOH544 2.5 15.7 1.0 CB A:CYS206 2.6 6.3 0.2 CB A:CYS206 2.8 6.9 0.8 HB3 A:CYS206 3.1 8.3 0.8 O A:VAL135 3.1 10.8 1.0 O A:GLN137 3.2 7.4 1.0 CE1 A:MBO307 3.3 10.8 0.8 HB3 A:LEU204 3.3 9.0 1.0 HB2 A:CYS206 3.3 7.5 0.2 HA A:CYS206 3.3 6.8 0.8 H A:GLN137 3.4 9.6 0.5 H A:GLN137 3.4 9.6 0.5 CA A:CYS206 3.5 5.7 0.8 CA A:CYS206 3.5 6.2 0.2 HA A:VAL135 3.5 11.2 1.0 C A:VAL135 3.5 9.0 1.0 HB2 A:CYS206 3.5 8.3 0.8 HA A:CYS206 3.6 7.4 0.2 N A:CYS206 3.6 6.2 0.2 N A:GLN137 3.7 8.0 1.0 N A:CYS206 3.7 5.9 0.8 C A:GLU205 3.8 6.6 1.0 O A:GLU205 3.8 8.0 1.0 HA A:GLN136 3.9 11.7 1.0 O A:HOH575 3.9 13.6 1.0 C A:GLN137 3.9 7.4 1.0 H A:GLU205 4.0 7.7 1.0 H A:CYS206 4.0 7.5 0.2 CE2 A:MBO307 4.1 11.2 0.8 C A:GLN136 4.1 9.1 1.0 CA A:VAL135 4.1 9.4 1.0 N A:GLN136 4.1 9.0 1.0 N A:GLU205 4.2 6.4 1.0 H A:CYS206 4.2 7.1 0.8 CB A:LEU204 4.2 7.5 1.0 CA A:GLN136 4.2 9.7 1.0 CE6 A:MBO307 4.3 10.9 0.8 HA A:PRO138 4.3 10.0 0.5 HB A:VAL135 4.3 12.5 1.0 HA A:PRO138 4.3 9.9 0.6 CA A:GLN137 4.4 7.8 1.0 HB2 A:LEU204 4.4 9.0 1.0 HD13 A:LEU204 4.5 13.1 1.0 C A:LEU204 4.6 5.8 1.0 O A:ALA134 4.6 8.1 1.0 CA A:GLU205 4.6 6.5 1.0 HD22 A:LEU204 4.6 14.3 1.0 O A:HOH639 4.7 34.9 1.0 N A:PRO138 4.7 7.7 0.6 N A:PRO138 4.7 7.8 0.5 H A:GLN136 4.8 10.8 1.0 CB A:VAL135 4.8 10.4 1.0 O A:GLN136 4.8 10.2 1.0 HA A:GLN137 4.9 9.3 1.0 C A:CYS206 4.9 6.0 0.2 CA A:LEU204 4.9 6.5 1.0 C A:CYS206 4.9 5.7 0.8 CA A:PRO138 5.0 8.3 0.6 CA A:PRO138 5.0 8.3 0.5

Mercury binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg307 b:9.7 occ:0.84 HG A:MBO307 0.0 9.7 0.8 HG A:HG302 1.3 7.6 0.2 CE1 A:MBO307 2.1 10.8 0.8 HB3 A:CYS206 2.2 7.5 0.2 SG A:CYS206 2.4 8.3 0.8 O A:GLN137 3.0 7.4 1.0 O A:HOH544 3.0 15.7 1.0 CE6 A:MBO307 3.0 10.9 0.8 CB A:CYS206 3.0 6.3 0.2 O A:GLU205 3.0 8.0 1.0 HA A:CYS206 3.1 6.8 0.8 CE2 A:MBO307 3.1 11.2 0.8 HA A:PRO138 3.3 10.0 0.5 HA A:CYS206 3.3 7.4 0.2 HA A:PRO138 3.3 9.9 0.6 C A:GLN137 3.4 7.4 1.0 C A:GLU205 3.4 6.6 1.0 CB A:CYS206 3.4 6.9 0.8 SG A:CYS206 3.5 6.7 0.2 CA A:CYS206 3.5 6.2 0.2 CA A:CYS206 3.5 5.7 0.8 HB3 A:CYS206 3.6 8.3 0.8 N A:CYS206 3.6 6.2 0.2 N A:CYS206 3.7 5.9 0.8 H A:GLN137 3.7 9.6 0.5 H A:GLN137 3.7 9.6 0.5 O A:HOH575 3.8 13.6 1.0 HB2 A:CYS206 3.8 7.5 0.2 N A:GLN137 3.8 8.0 1.0 N A:PRO138 3.9 7.7 0.6 N A:PRO138 3.9 7.8 0.5 H A:GLU205 4.0 7.7 1.0 CA A:PRO138 4.0 8.3 0.5 CA A:PRO138 4.0 8.3 0.6 CA A:GLN137 4.1 7.8 1.0 HB3 A:LEU204 4.2 9.0 1.0 C A:GLN136 4.2 9.1 1.0 N A:GLU205 4.2 6.4 1.0 O A:VAL135 4.2 10.8 1.0 HB2 A:CYS206 4.3 8.3 0.8 H A:CYS206 4.3 7.5 0.2 CA A:GLU205 4.3 6.5 1.0 CE5 A:MBO307 4.4 11.7 0.8 H A:CYS206 4.4 7.1 0.8 HA A:GLN136 4.4 11.7 1.0 CE3 A:MBO307 4.4 11.4 0.8 HA A:GLN137 4.5 9.3 1.0 HB2 A:GLU205 4.5 8.1 1.0 O A:HOH639 4.6 34.9 1.0 C A:VAL135 4.6 9.0 1.0 HA A:VAL135 4.7 11.2 1.0 HD3 A:PRO138 4.7 10.3 0.6 O A:GLN136 4.7 10.2 1.0 CA A:GLN136 4.7 9.7 1.0 HB3 A:PRO138 4.7 11.7 0.5 HD3 A:PRO138 4.8 10.6 0.5 HG3 A:PRO138 4.8 11.1 0.6 CD A:PRO138 4.8 8.6 0.6 C A:PRO138 4.9 7.0 0.6 O A:HOH633 4.9 29.5 1.0 CE4 A:MBO307 4.9 11.9 0.8 N A:GLN136 4.9 9.0 1.0 CB A:GLU205 4.9 6.8 1.0 C A:LEU204 5.0 5.8 1.0 CD A:PRO138 5.0 8.8 0.5 C A:CYS206 5.0 5.7 0.8 C A:CYS206 5.0 6.0 0.2 C A:PRO138 5.0 7.5 0.5

S.Gloeckner, A.Heine, G.Klebe. Human Carbonic Anhydrase II in Complex with 4-Methylbenzenesulfonamide To Be Published.