Mercury in PDB 6sbm: Human Carbonic Anhydrase II in Complex with 4-(Pentyloxy) Benzenesulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with 4-(Pentyloxy) Benzenesulfonamide:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with 4-(Pentyloxy) Benzenesulfonamide, PDB code: 6sbm 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)	39.93 / 0.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.348, 41.603, 71.968, 90.00, 104.24, 90.00
R / Rfree (%)	11.7 / 12.8

The structure of Human Carbonic Anhydrase II in Complex with 4-(Pentyloxy) Benzenesulfonamide also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Sodium	(Na)	2 atoms

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


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-(Pentyloxy) Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg307 b:9.9 occ:0.32 HG A:BE7307 0.0 9.9 0.3 HG A:BE7307 1.1 7.9 0.5 C5 A:BE7307 1.6 7.6 0.5 C5 A:BE7307 2.1 10.8 0.3 C6 A:BE7307 2.1 8.4 0.5 HB3 A:CYS206 2.2 12.8 0.2 SG A:CYS206 2.6 11.5 0.3 C4 A:BE7307 2.8 9.9 0.5 O A:GLN137 2.9 7.6 0.5 O A:GLU205 3.0 9.4 1.0 O A:GLN137 3.0 8.8 0.5 C6 A:BE7307 3.0 12.3 0.3 C4 A:BE7307 3.0 11.7 0.3 HA A:CYS206 3.1 7.0 0.5 HA A:CYS206 3.1 9.7 0.3 CB A:CYS206 3.1 10.6 0.2 SG A:CYS206 3.2 7.8 0.5 HA A:CYS206 3.2 10.4 0.2 HA A:PRO138 3.3 10.3 1.0 C A:GLU205 3.3 7.0 1.0 C A:GLN137 3.4 7.4 0.5 C A:GLN137 3.4 8.5 0.5 C7 A:BE7307 3.5 10.6 0.5 CA A:CYS206 3.5 8.7 0.2 CA A:CYS206 3.5 5.9 0.5 O A:HOH547 3.6 19.5 1.0 N A:CYS206 3.6 5.8 0.5 CB A:CYS206 3.6 10.6 0.3 CA A:CYS206 3.6 8.1 0.3 N A:CYS206 3.6 7.7 0.2 CB A:CYS206 3.6 7.3 0.5 N A:CYS206 3.7 7.1 0.3 H A:GLN137 3.7 11.2 0.5 HB3 A:CYS206 3.7 8.8 0.5 HB2 A:CYS206 3.7 12.8 0.2 H A:GLU205 3.7 8.6 1.0 H A:GLN137 3.7 10.2 0.5 N A:GLN137 3.8 9.3 0.5 N A:GLN137 3.8 8.5 0.5 HB3 A:LEU204 3.8 10.5 1.0 N A:PRO138 3.9 8.3 1.0 HB3 A:CYS206 3.9 12.8 0.3 O A:VAL135 3.9 11.2 1.0 C3 A:BE7307 4.0 11.6 0.5 N A:GLU205 4.0 7.2 1.0 CA A:PRO138 4.0 8.6 1.0 CA A:GLN137 4.1 7.8 0.5 CA A:GLN137 4.1 9.4 0.5 CA A:GLU205 4.2 7.4 1.0 H A:CYS206 4.2 7.0 0.5 H A:CYS206 4.2 9.2 0.2 C2 A:BE7307 4.2 12.0 0.5 C A:GLN136 4.3 9.8 1.0 SG A:CYS206 4.3 12.7 0.2 H A:CYS206 4.3 8.5 0.3 C7 A:BE7307 4.3 12.5 0.3 C3 A:BE7307 4.3 12.1 0.3 HB2 A:CYS206 4.4 12.8 0.3 HA A:GLN136 4.4 12.5 1.0 HB2 A:GLU205 4.4 9.7 1.0 HA A:GLN137 4.4 9.3 0.5 HA A:GLN137 4.4 11.3 0.5 C A:VAL135 4.5 9.9 1.0 HB2 A:CYS206 4.6 8.8 0.5 HG A:CYS206 4.6 15.2 0.2 HD3 A:PRO138 4.7 12.1 1.0 C A:LEU204 4.7 7.0 1.0 HB3 A:PRO138 4.7 12.5 1.0 HA A:VAL135 4.7 11.5 1.0 CB A:LEU204 4.7 8.8 1.0 CA A:GLN136 4.8 10.4 1.0 O A:GLN136 4.8 10.8 1.0 CB A:GLU205 4.8 8.1 1.0 C2 A:BE7307 4.9 12.9 0.3 CD A:PRO138 4.9 10.0 1.0 N A:GLN136 4.9 9.6 1.0 HD22 A:LEU204 5.0 16.6 1.0 HA A:GLU205 5.0 8.9 1.0 CB A:PRO138 5.0 10.4 1.0 C A:PRO138 5.0 7.9 1.0

Mercury binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with 4-(Pentyloxy) Benzenesulfonamide


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-(Pentyloxy) Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg307 b:7.9 occ:0.52 HG A:BE7307 0.0 7.9 0.5 HG A:BE7307 1.1 9.9 0.3 SG A:CYS206 1.7 11.5 0.3 HB3 A:CYS206 1.7 12.8 0.2 C5 A:BE7307 2.0 7.6 0.5 SG A:CYS206 2.3 7.8 0.5 CB A:CYS206 2.7 10.6 0.2 C4 A:BE7307 3.0 9.9 0.5 O A:VAL135 3.0 11.2 1.0 C6 A:BE7307 3.0 8.4 0.5 O A:GLN137 3.1 7.6 0.5 CB A:CYS206 3.1 10.6 0.3 C5 A:BE7307 3.1 10.8 0.3 O A:GLN137 3.1 8.8 0.5 CB A:CYS206 3.2 7.3 0.5 HB3 A:LEU204 3.2 10.5 1.0 HB3 A:CYS206 3.2 8.8 0.5 HB2 A:CYS206 3.2 12.8 0.2 H A:GLN137 3.3 11.2 0.5 HA A:CYS206 3.3 7.0 0.5 H A:GLN137 3.3 10.2 0.5 HA A:CYS206 3.3 9.7 0.3 HB3 A:CYS206 3.4 12.8 0.3 HA A:CYS206 3.5 10.4 0.2 CA A:CYS206 3.5 8.7 0.2 CA A:CYS206 3.5 5.9 0.5 SG A:CYS206 3.6 12.7 0.2 CA A:CYS206 3.6 8.1 0.3 C A:VAL135 3.6 9.9 1.0 N A:GLN137 3.6 9.3 0.5 HG A:CYS206 3.6 15.2 0.2 N A:CYS206 3.6 5.8 0.5 N A:GLN137 3.6 8.5 0.5 N A:CYS206 3.7 7.7 0.2 C A:GLU205 3.7 7.0 1.0 O A:GLU205 3.7 9.4 1.0 C A:GLN137 3.7 7.4 0.5 HA A:VAL135 3.7 11.5 1.0 C A:GLN137 3.7 8.5 0.5 N A:CYS206 3.7 7.1 0.3 HB2 A:CYS206 3.8 12.8 0.3 C4 A:BE7307 3.9 11.7 0.3 H A:GLU205 3.9 8.6 1.0 O A:HOH547 3.9 19.5 1.0 HA A:GLN136 3.9 12.5 1.0 HB2 A:CYS206 4.0 8.8 0.5 N A:GLU205 4.1 7.2 1.0 HA A:PRO138 4.1 10.3 1.0 H A:CYS206 4.1 7.0 0.5 C A:GLN136 4.1 9.8 1.0 CB A:LEU204 4.1 8.8 1.0 C6 A:BE7307 4.1 12.3 0.3 H A:CYS206 4.1 9.2 0.2 CA A:VAL135 4.2 9.6 1.0 N A:GLN136 4.2 9.6 1.0 H A:CYS206 4.3 8.5 0.3 CA A:GLN137 4.3 9.4 0.5 CA A:GLN137 4.3 7.8 0.5 C3 A:BE7307 4.3 11.6 0.5 HB2 A:LEU204 4.3 10.5 1.0 CA A:GLN136 4.3 10.4 1.0 HD13 A:LEU204 4.3 15.4 1.0 C7 A:BE7307 4.3 10.6 0.5 C A:LEU204 4.5 7.0 1.0 HD22 A:LEU204 4.5 16.6 1.0 CA A:GLU205 4.5 7.4 1.0 N A:PRO138 4.5 8.3 1.0 HB A:VAL135 4.5 12.6 1.0 O A:ALA134 4.6 9.1 1.0 HA A:GLN137 4.7 9.3 0.5 HA A:GLN137 4.7 11.3 0.5 CA A:PRO138 4.8 8.6 1.0 CA A:LEU204 4.8 7.5 1.0 C2 A:BE7307 4.8 12.0 0.5 O A:GLN136 4.9 10.8 1.0 H A:GLN136 4.9 11.6 1.0 C A:CYS206 4.9 7.9 0.2 HA A:LEU204 5.0 9.0 1.0 CB A:VAL135 5.0 10.5 1.0 C A:CYS206 5.0 6.3 0.5 O A:HOH509 5.0 26.2 1.0

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