Mercury in PDB 5ll8: Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor., PDB code: 5ll8 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)	40.98 / 1.03
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.280, 41.450, 71.980, 90.00, 104.22, 90.00
R / Rfree (%)	12 / 14.3

The structure of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor. 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 Aliphatic Benzenesulfonamide Inhibitor. (pdb code 5ll8). 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 Aliphatic Benzenesulfonamide Inhibitor., PDB code: 5ll8:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.


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 Aliphatic Benzenesulfonamide Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg307 b:11.6 occ:0.40 HG A:BE7307 0.0 11.6 0.4 HG A:HG308 1.3 9.6 0.1 C5 A:BE7307 2.1 11.5 0.4 SG A:CYS206 2.4 9.3 0.4 HB3 A:CYS206 2.4 8.2 0.5 O A:HOH497 2.5 12.8 0.6 HA A:CYS206 2.9 8.4 0.1 O A:GLN137 3.0 8.8 1.0 C4 A:BE7307 3.0 11.8 0.4 C6 A:BE7307 3.0 12.3 0.4 O A:GLU205 3.0 8.6 1.0 HA A:CYS206 3.1 8.8 0.4 HA A:CYS206 3.1 7.4 0.5 CB A:CYS206 3.2 6.9 0.5 C A:GLN137 3.3 8.8 1.0 HA A:PRO138 3.3 11.4 0.5 HA A:PRO138 3.3 11.5 0.5 CB A:CYS206 3.3 8.5 0.4 SG A:CYS206 3.4 7.6 0.1 C A:GLU205 3.4 7.2 1.0 O A:VAL135 3.4 10.6 0.6 HB3 A:CYS206 3.5 10.2 0.4 CA A:CYS206 3.5 7.3 0.4 CA A:CYS206 3.5 6.2 0.5 CA A:CYS206 3.6 7.0 0.1 N A:GLN137 3.6 9.9 1.0 HB2 A:CYS206 3.6 8.2 0.5 H A:GLN137 3.6 11.9 1.0 N A:CYS206 3.7 7.1 0.1 N A:CYS206 3.7 7.2 0.4 O A:HOH587 3.7 19.6 1.0 N A:CYS206 3.7 6.5 0.5 N A:PRO138 3.8 9.1 1.0 C A:GLN136 3.8 12.3 1.0 CB A:CYS206 3.9 7.4 0.1 CA A:GLN137 3.9 8.9 1.0 H A:GLU205 4.0 8.6 1.0 CA A:PRO138 4.0 9.5 0.5 CA A:PRO138 4.0 9.6 0.5 HB3 A:LEU204 4.0 10.4 1.0 HA A:GLN136 4.0 16.0 1.0 HB3 A:CYS206 4.1 8.8 0.1 HB2 A:CYS206 4.2 10.2 0.4 N A:GLU205 4.2 7.1 1.0 HA A:GLN137 4.2 10.7 1.0 O A:VAL135 4.2 12.9 0.4 O A:GLN136 4.2 14.3 1.0 C A:VAL135 4.3 11.7 0.6 H A:CYS206 4.3 8.5 0.1 H A:CYS206 4.3 8.6 0.4 C3 A:BE7307 4.3 12.4 0.4 CA A:GLU205 4.3 7.0 1.0 C7 A:BE7307 4.3 12.6 0.4 H A:CYS206 4.4 7.8 0.5 CA A:GLN136 4.4 13.3 1.0 HD3 A:PRO138 4.4 12.2 0.5 HD3 A:PRO138 4.5 12.2 0.5 HB2 A:GLU205 4.5 8.9 1.0 C A:VAL135 4.5 12.3 0.4 HG3 A:PRO138 4.6 13.0 0.5 CD A:PRO138 4.6 10.2 0.5 SG A:CYS206 4.7 7.2 0.5 N A:GLN136 4.7 12.2 1.0 CD A:PRO138 4.7 10.2 0.5 HB3 A:PRO138 4.8 12.8 0.5 HB2 A:CYS206 4.8 8.8 0.1 HA A:VAL135 4.8 13.2 0.4 C2 A:BE7307 4.9 13.0 0.4 C A:LEU204 4.9 7.3 1.0 C A:PRO138 4.9 9.2 1.0 CB A:GLU205 4.9 7.4 1.0 CB A:LEU204 5.0 8.7 1.0 C A:CYS206 5.0 6.9 0.1 C A:CYS206 5.0 6.2 0.5 C A:CYS206 5.0 6.9 0.4

Mercury binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.


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 Aliphatic Benzenesulfonamide Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg308 b:9.6 occ:0.15 HG A:BE7307 1.3 11.6 0.4 SG A:CYS206 1.3 9.3 0.4 HB3 A:CYS206 1.7 8.2 0.5 O A:HOH497 2.1 12.8 0.6 O A:VAL135 2.2 10.6 0.6 SG A:CYS206 2.3 7.6 0.1 CB A:CYS206 2.6 6.9 0.5 CB A:CYS206 2.7 8.5 0.4 HB3 A:CYS206 2.9 10.2 0.4 HB2 A:CYS206 3.0 8.2 0.5 O A:VAL135 3.1 12.9 0.4 HA A:CYS206 3.1 8.4 0.1 HB3 A:LEU204 3.2 10.4 1.0 C A:VAL135 3.2 11.7 0.6 O A:GLN137 3.2 8.8 1.0 H A:GLN137 3.2 11.9 1.0 CB A:CYS206 3.3 7.4 0.1 C5 A:BE7307 3.3 11.5 0.4 HA A:CYS206 3.4 8.8 0.4 HA A:CYS206 3.4 7.4 0.5 C A:VAL135 3.4 12.3 0.4 HB2 A:CYS206 3.4 10.2 0.4 HA A:GLN136 3.4 16.0 1.0 CA A:CYS206 3.4 6.2 0.5 N A:GLN137 3.4 9.9 1.0 CA A:CYS206 3.5 7.3 0.4 CA A:CYS206 3.5 7.0 0.1 HB3 A:CYS206 3.5 8.8 0.1 N A:CYS206 3.7 7.1 0.1 N A:CYS206 3.7 7.2 0.4 C A:GLN136 3.7 12.3 1.0 HA A:VAL135 3.7 13.2 0.4 N A:CYS206 3.7 6.5 0.5 SG A:CYS206 3.8 7.2 0.5 C A:GLN137 3.8 8.8 1.0 C A:GLU205 3.8 7.2 1.0 O A:GLU205 3.8 8.6 1.0 CA A:GLN136 3.8 13.3 1.0 N A:GLN136 3.9 12.2 1.0 HA A:VAL135 3.9 12.8 0.6 O A:HOH587 3.9 19.6 1.0 H A:GLU205 4.0 8.6 1.0 C6 A:BE7307 4.1 12.3 0.4 CB A:LEU204 4.1 8.7 1.0 H A:CYS206 4.1 8.5 0.1 H A:CYS206 4.1 8.6 0.4 HB2 A:CYS206 4.1 8.8 0.1 CA A:VAL135 4.1 11.0 0.4 CA A:VAL135 4.2 10.7 0.6 N A:GLU205 4.2 7.1 1.0 H A:CYS206 4.2 7.8 0.5 CA A:GLN137 4.2 8.9 1.0 HA A:PRO138 4.3 11.4 0.5 HA A:PRO138 4.3 11.5 0.5 C4 A:BE7307 4.3 11.8 0.4 HD13 A:LEU204 4.3 14.0 1.0 HB2 A:LEU204 4.3 10.4 1.0 O A:GLN136 4.4 14.3 1.0 HD22 A:LEU204 4.5 15.2 1.0 HB A:VAL135 4.5 13.0 0.6 C A:LEU204 4.5 7.3 1.0 O A:ALA134 4.6 8.6 1.0 HB A:VAL135 4.6 13.5 0.4 H A:GLN136 4.6 14.6 1.0 N A:PRO138 4.6 9.1 1.0 CA A:GLU205 4.6 7.0 1.0 HA A:GLN137 4.6 10.7 1.0 C A:CYS206 4.8 6.2 0.5 CA A:LEU204 4.8 7.6 1.0 C A:CYS206 4.9 6.9 0.4 CA A:PRO138 4.9 9.5 0.5 CB A:VAL135 4.9 10.8 0.6 CA A:PRO138 4.9 9.6 0.5 C A:CYS206 4.9 6.9 0.1 CG A:LEU204 5.0 10.8 1.0 HA A:LEU204 5.0 9.1 1.0 CB A:VAL135 5.0 11.2 0.4

S.Gloeckner, A.Heine, G.Klebe. Crystallographic, Kinetic and Thermodynamic Characterization of Aliphatic Benzenesulfonamides As Ligands of Human Carbonic Anhydrase II To Be Published.