Mercury in PDB 6hr3: Human Carbonic Anhydrase II in Complex with 4-Propylbenzenesulfonamide

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

The structure of Human Carbonic Anhydrase II in Complex with 4-Propylbenzenesulfonamide, PDB code: 6hr3 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)	34.98 / 1.02
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.270, 41.519, 72.293, 90.00, 104.59, 90.00
R / Rfree (%)	12.9 / 14.5

The structure of Human Carbonic Anhydrase II in Complex with 4-Propylbenzenesulfonamide 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-Propylbenzenesulfonamide (pdb code 6hr3). 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-Propylbenzenesulfonamide, PDB code: 6hr3:
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-Propylbenzenesulfonamide


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-Propylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg303 b:10.8 occ:0.70 HG A:MBO303 0.0 10.8 0.7 HG A:HG304 1.3 13.4 0.3 CE1 A:MBO303 2.1 11.1 0.7 HB3 A:CYS206 2.3 11.1 0.1 HB3 A:CYS206 2.3 10.5 0.2 SG A:CYS206 2.4 9.2 0.7 O A:HOH533 2.9 19.6 1.0 O A:GLN137 3.0 9.9 1.0 CB A:CYS206 3.0 8.7 0.2 CE6 A:MBO303 3.0 12.1 0.7 O A:GLU205 3.0 9.9 1.0 HA A:CYS206 3.0 9.1 0.7 CE2 A:MBO303 3.1 12.6 0.7 HA A:CYS206 3.1 10.0 0.1 CB A:CYS206 3.2 9.3 0.1 HA A:PRO138 3.2 12.5 0.5 HA A:CYS206 3.2 9.9 0.2 HA A:PRO138 3.3 12.2 0.5 C A:GLN137 3.4 9.4 1.0 SG A:CYS206 3.4 8.8 0.2 C A:GLU205 3.4 8.3 1.0 CB A:CYS206 3.4 8.6 0.7 CA A:CYS206 3.5 8.3 0.2 CA A:CYS206 3.5 8.3 0.1 CA A:CYS206 3.5 7.6 0.7 HB2 A:CYS206 3.6 11.1 0.1 N A:CYS206 3.6 8.3 0.2 HB3 A:CYS206 3.6 10.4 0.7 N A:CYS206 3.7 8.2 0.1 H A:GLN137 3.7 12.4 0.5 N A:CYS206 3.7 7.8 0.7 O A:HOH565 3.8 16.9 1.0 H A:GLN137 3.8 12.4 0.5 N A:GLN137 3.8 10.3 1.0 HB2 A:CYS206 3.9 10.5 0.2 N A:PRO138 3.9 9.6 0.5 N A:PRO138 3.9 9.8 0.5 H A:GLU205 4.0 10.1 1.0 CA A:PRO138 4.0 10.4 0.5 CA A:PRO138 4.0 10.2 0.5 C A:GLN136 4.1 11.5 0.5 CA A:GLN137 4.1 9.7 1.0 HB3 A:LEU204 4.2 11.5 1.0 O A:VAL135 4.2 13.7 1.0 N A:GLU205 4.2 8.4 1.0 C A:GLN136 4.2 11.2 0.5 H A:CYS206 4.2 10.0 0.2 HB2 A:CYS206 4.3 10.4 0.7 H A:CYS206 4.3 9.9 0.1 HA A:GLN136 4.4 14.0 0.5 CA A:GLU205 4.4 8.2 1.0 HA A:GLN136 4.4 14.3 0.5 H A:CYS206 4.4 9.4 0.7 CE5 A:MBO303 4.4 12.3 0.7 CE3 A:MBO303 4.4 12.6 0.7 O A:HOH612 4.4 45.9 1.0 HA A:GLN137 4.4 11.6 1.0 O A:GLN136 4.5 12.1 0.5 SG A:CYS206 4.5 10.6 0.1 HB2 A:GLU205 4.5 10.4 1.0 C A:VAL135 4.6 10.9 1.0 HD3 A:PRO138 4.6 12.7 0.5 HB3 A:PRO138 4.7 14.1 0.5 HA A:VAL135 4.7 13.8 1.0 CA A:GLN136 4.7 11.9 0.5 CA A:GLN136 4.7 11.7 0.5 O A:GLN136 4.8 11.6 0.5 HD3 A:PRO138 4.8 13.4 0.5 CD A:PRO138 4.8 10.6 0.5 C A:PRO138 4.8 9.1 0.5 N A:GLN136 4.9 11.5 0.5 O A:HOH613 4.9 28.7 1.0 N A:GLN136 4.9 11.4 0.5 CE4 A:MBO303 4.9 12.2 0.7 HG3 A:PRO138 5.0 13.4 0.5 CD A:PRO138 5.0 11.2 0.5 C A:CYS206 5.0 7.8 0.1 CB A:PRO138 5.0 11.7 0.5 C A:CYS206 5.0 7.8 0.2 CB A:GLU205 5.0 8.7 1.0 C A:PRO138 5.0 9.6 0.5 C A:CYS206 5.0 7.7 0.7 C A:LEU204 5.0 7.9 1.0

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


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-Propylbenzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg304 b:13.4 occ:0.30 HG A:MBO303 1.3 10.8 0.7 SG A:CYS206 1.3 9.2 0.7 HB3 A:CYS206 1.7 11.1 0.1 HB3 A:CYS206 2.1 10.5 0.2 SG A:CYS206 2.3 8.8 0.2 O A:HOH533 2.5 19.6 1.0 CB A:CYS206 2.6 8.7 0.2 CB A:CYS206 2.7 9.3 0.1 CB A:CYS206 2.9 8.6 0.7 HB2 A:CYS206 3.1 11.1 0.1 HB3 A:CYS206 3.1 10.4 0.7 O A:VAL135 3.1 13.7 1.0 HB3 A:LEU204 3.3 11.5 1.0 O A:GLN137 3.3 9.9 1.0 CE1 A:MBO303 3.3 11.1 0.7 HA A:CYS206 3.3 9.1 0.7 HB2 A:CYS206 3.4 10.5 0.2 H A:GLN137 3.4 12.4 0.5 HA A:CYS206 3.5 10.0 0.1 CA A:CYS206 3.5 8.3 0.1 CA A:CYS206 3.5 8.3 0.2 CA A:CYS206 3.5 7.6 0.7 H A:GLN137 3.5 12.4 0.5 HB2 A:CYS206 3.6 10.4 0.7 C A:VAL135 3.6 10.9 1.0 HA A:CYS206 3.6 9.9 0.2 HA A:VAL135 3.6 13.8 1.0 N A:CYS206 3.6 8.3 0.2 SG A:CYS206 3.6 10.6 0.1 N A:CYS206 3.7 8.2 0.1 N A:CYS206 3.7 7.8 0.7 N A:GLN137 3.7 10.3 1.0 C A:GLU205 3.8 8.3 1.0 O A:GLU205 3.8 9.9 1.0 O A:HOH565 3.8 16.9 1.0 HA A:GLN136 3.9 14.0 0.5 HA A:GLN136 3.9 14.3 0.5 C A:GLN137 3.9 9.4 1.0 H A:GLU205 3.9 10.1 1.0 H A:CYS206 4.0 10.0 0.2 C A:GLN136 4.1 11.5 0.5 CE2 A:MBO303 4.1 12.6 0.7 H A:CYS206 4.1 9.9 0.1 N A:GLU205 4.1 8.4 1.0 CA A:VAL135 4.2 11.5 1.0 N A:GLN136 4.2 11.5 0.5 C A:GLN136 4.2 11.2 0.5 N A:GLN136 4.2 11.4 0.5 CB A:LEU204 4.2 9.6 1.0 H A:CYS206 4.2 9.4 0.7 CA A:GLN136 4.2 11.9 0.5 HA A:PRO138 4.3 12.5 0.5 CA A:GLN136 4.3 11.7 0.5 CE6 A:MBO303 4.3 12.1 0.7 HA A:PRO138 4.4 12.2 0.5 HB2 A:LEU204 4.4 11.5 1.0 HB A:VAL135 4.4 16.0 1.0 HD13 A:LEU204 4.4 16.1 1.0 CA A:GLN137 4.4 9.7 1.0 C A:LEU204 4.5 7.9 1.0 CA A:GLU205 4.6 8.2 1.0 O A:HOH612 4.6 45.9 1.0 HD22 A:LEU204 4.6 18.1 1.0 O A:HOH540 4.7 42.0 1.0 O A:ALA134 4.7 10.2 1.0 O A:GLN136 4.7 12.1 0.5 N A:PRO138 4.7 9.6 0.5 N A:PRO138 4.8 9.8 0.5 H A:GLN136 4.8 13.8 0.5 H A:GLN136 4.8 13.7 0.5 CB A:VAL135 4.9 13.4 1.0 C A:CYS206 4.9 7.8 0.2 CA A:LEU204 4.9 8.4 1.0 C A:CYS206 4.9 7.8 0.1 HA A:GLN137 4.9 11.6 1.0 C A:CYS206 4.9 7.7 0.7 O A:GLN136 5.0 11.6 0.5 CA A:PRO138 5.0 10.4 0.5 CA A:PRO138 5.0 10.2 0.5

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