Mercury in PDB 6i3e: Human Carbonic Anhydrase II in Complex with 4-Butylbenzenesulfonamide

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

The structure of Human Carbonic Anhydrase II in Complex with 4-Butylbenzenesulfonamide, PDB code: 6i3e was solved by S.Gloeckner, K.Ngo, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.18 / 1.07
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.483, 41.487, 71.915, 90.00, 104.22, 90.00
R / Rfree (%)	12.9 / 14.7

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

Zinc	(Zn)	1 atom
Sodium	(Na)	3 atoms

The binding sites of Mercury atom in the Human Carbonic Anhydrase II in Complex with 4-Butylbenzenesulfonamide (pdb code 6i3e). 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-Butylbenzenesulfonamide, PDB code: 6i3e:
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-Butylbenzenesulfonamide


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-Butylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg306 b:11.2 occ:0.40 HG A:MBO307 1.0 9.3 0.6 CE1 A:MBO307 1.6 12.0 0.6 CE2 A:MBO307 2.1 13.8 0.6 SG A:CYS206 2.4 9.8 0.4 CE6 A:MBO307 2.9 12.6 0.6 O A:GLN137 2.9 8.3 1.0 HA A:CYS206 3.1 8.6 0.6 O A:GLU205 3.1 9.9 1.0 HA A:CYS206 3.2 9.4 0.4 SG A:CYS206 3.2 8.0 0.6 HA A:PRO138 3.3 10.5 1.0 C A:GLN137 3.3 8.3 1.0 CB A:CYS206 3.4 9.5 0.4 C A:GLU205 3.4 8.0 1.0 HB3 A:CYS206 3.5 11.4 0.4 CE3 A:MBO307 3.5 13.8 0.6 CA A:CYS206 3.5 7.8 0.4 H A:GLN137 3.5 11.1 1.0 CA A:CYS206 3.6 7.2 0.6 N A:CYS206 3.6 6.8 0.6 N A:CYS206 3.6 7.2 0.4 CB A:CYS206 3.7 7.8 0.6 N A:GLN137 3.7 9.2 1.0 H A:GLU205 3.7 9.0 1.0 O A:HOH545 3.7 19.9 1.0 HB3 A:CYS206 3.7 9.4 0.6 HB3 A:LEU204 3.7 12.3 1.0 O A:VAL135 3.9 11.0 1.0 N A:PRO138 3.9 8.6 1.0 N A:GLU205 4.0 7.5 1.0 CE5 A:MBO307 4.0 13.3 0.6 CA A:GLN137 4.0 8.7 1.0 CA A:PRO138 4.0 8.8 1.0 C A:GLN136 4.1 9.7 1.0 H A:CYS206 4.2 8.1 0.6 H A:CYS206 4.2 8.6 0.4 HB2 A:CYS206 4.2 11.4 0.4 CA A:GLU205 4.2 7.6 1.0 CE4 A:MBO307 4.2 14.2 0.6 O A:HOH528 4.3 22.9 1.0 HA A:GLN137 4.3 10.4 1.0 HA A:GLN136 4.4 12.9 1.0 C A:VAL135 4.4 9.7 1.0 HB2 A:GLU205 4.5 9.7 1.0 HD3 A:PRO138 4.6 12.4 1.0 HB2 A:CYS206 4.6 9.4 0.6 HA A:VAL135 4.6 12.1 1.0 CB A:LEU204 4.7 10.3 1.0 C A:LEU204 4.7 7.3 1.0 O A:GLN136 4.7 11.1 1.0 CA A:GLN136 4.7 10.8 1.0 HB3 A:PRO138 4.7 13.0 1.0 N A:GLN136 4.8 9.5 1.0 CD A:PRO138 4.8 10.3 1.0 HB2 A:LEU204 4.9 12.3 1.0 CB A:GLU205 4.9 8.0 1.0 HD22 A:LEU204 5.0 17.0 1.0

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


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-Butylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg307 b:9.3 occ:0.60 HG A:MBO307 0.0 9.3 0.6 HG A:HG306 1.0 11.2 0.4 SG A:CYS206 1.6 9.8 0.4 CE1 A:MBO307 2.1 12.0 0.6 SG A:CYS206 2.4 8.0 0.6 CB A:CYS206 2.9 9.5 0.4 O A:VAL135 3.0 11.0 1.0 CE6 A:MBO307 3.0 12.6 0.6 CE2 A:MBO307 3.0 13.8 0.6 O A:GLN137 3.1 8.3 1.0 HB3 A:CYS206 3.1 11.4 0.4 HB3 A:LEU204 3.1 12.3 1.0 CB A:CYS206 3.2 7.8 0.6 H A:GLN137 3.3 11.1 1.0 HA A:CYS206 3.3 8.6 0.6 HB3 A:CYS206 3.3 9.4 0.6 HA A:CYS206 3.4 9.4 0.4 CA A:CYS206 3.5 7.8 0.4 C A:VAL135 3.6 9.7 1.0 CA A:CYS206 3.6 7.2 0.6 N A:GLN137 3.6 9.2 1.0 N A:CYS206 3.7 6.8 0.6 N A:CYS206 3.7 7.2 0.4 HB2 A:CYS206 3.7 11.4 0.4 HA A:VAL135 3.7 12.1 1.0 C A:GLN137 3.7 8.3 1.0 C A:GLU205 3.8 8.0 1.0 O A:GLU205 3.8 9.9 1.0 H A:GLU205 3.8 9.0 1.0 HA A:GLN136 3.9 12.9 1.0 O A:HOH545 4.0 19.9 1.0 CB A:LEU204 4.0 10.3 1.0 C A:GLN136 4.0 9.7 1.0 N A:GLU205 4.0 7.5 1.0 H A:CYS206 4.1 8.1 0.6 HA A:PRO138 4.1 10.5 1.0 H A:CYS206 4.1 8.6 0.4 HB2 A:CYS206 4.1 9.4 0.6 HB2 A:LEU204 4.2 12.3 1.0 N A:GLN136 4.2 9.5 1.0 CA A:VAL135 4.2 10.1 1.0 CA A:GLN137 4.2 8.7 1.0 CA A:GLN136 4.3 10.8 1.0 HD13 A:LEU204 4.3 16.4 1.0 CE5 A:MBO307 4.3 13.3 0.6 CE3 A:MBO307 4.3 13.8 0.6 C A:LEU204 4.4 7.3 1.0 HD22 A:LEU204 4.5 17.0 1.0 HB A:VAL135 4.5 13.0 1.0 CA A:GLU205 4.5 7.6 1.0 N A:PRO138 4.5 8.6 1.0 O A:ALA134 4.6 8.7 1.0 HA A:GLN137 4.7 10.4 1.0 CA A:LEU204 4.8 8.6 1.0 CA A:PRO138 4.8 8.8 1.0 O A:GLN136 4.8 11.1 1.0 CE4 A:MBO307 4.9 14.2 0.6 H A:GLN136 4.9 11.4 1.0 HA A:LEU204 4.9 10.3 1.0 CG A:LEU204 5.0 12.9 1.0 C A:CYS206 5.0 7.5 0.4 O A:LEU204 5.0 7.2 1.0 CB A:VAL135 5.0 10.8 1.0

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