Mercury in PDB 4q78: Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase

All present enzymatic activity of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase:
4.2.1.1;

The structure of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase, PDB code: 4q78 was solved by P.Mader, J.Brynda, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.90 / 1.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.200, 41.725, 72.155, 90.00, 104.36, 90.00
R / Rfree (%)	17.5 / 20.1

The structure of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase (pdb code 4q78). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase, PDB code: 4q78:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg303 b:21.5 occ:0.70 HG A:MBO303 0.0 21.5 0.7 HG A:MBO303 0.8 4.0 0.2 HG A:MBO304 1.1 15.8 0.1 SG A:CYS206 1.8 8.8 0.6 CE1 A:MBO303 2.2 15.6 0.7 O A:HOH507 2.7 20.0 1.0 SG A:CYS206 2.8 8.0 0.2 CB A:CYS206 2.9 7.3 0.2 CE1 A:MBO303 3.0 3.6 0.2 CB A:CYS206 3.0 9.3 0.6 O A:GLN137 3.1 8.6 1.0 CB A:CYS206 3.1 7.8 0.2 CE6 A:MBO303 3.1 16.5 0.7 CE2 A:MBO303 3.1 15.8 0.7 O A:GLU205 3.4 9.1 1.0 CA A:CYS206 3.5 7.0 0.2 CA A:CYS206 3.5 7.2 0.6 CA A:CYS206 3.5 7.1 0.2 O A:VAL135 3.5 13.7 1.0 C A:GLN137 3.6 8.0 1.0 C A:GLU205 3.6 7.5 1.0 N A:GLN137 3.6 8.9 1.0 N A:CYS206 3.7 7.3 1.0 CE6 A:MBO303 3.7 4.6 0.2 O A:HOH456 3.8 19.8 1.0 CE2 A:MBO303 3.9 3.7 0.2 C A:VAL135 3.9 11.5 1.0 SG A:CYS206 4.1 8.2 0.2 C A:GLN136 4.1 10.1 1.0 CA A:GLN137 4.2 8.5 1.0 N A:GLU205 4.2 8.8 1.0 N A:PRO138 4.3 8.2 1.0 CA A:GLN136 4.4 10.9 1.0 N A:GLN136 4.4 10.5 1.0 CE3 A:MBO303 4.4 19.5 0.7 CE5 A:MBO303 4.4 18.4 0.7 CA A:GLU205 4.5 8.0 1.0 CA A:PRO138 4.5 8.9 1.0 CB A:LEU204 4.6 10.4 1.0 CA A:VAL135 4.6 10.8 1.0 C A:LEU204 4.7 7.8 1.0 O A:GLN136 4.7 12.2 1.0 O A:ALA134 4.9 8.7 1.0 CE4 A:MBO303 4.9 21.3 0.7 C A:CYS206 4.9 7.0 1.0

Mercury binding site 2 out of 3 in the Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg303 b:4.0 occ:0.20 HG A:MBO303 0.0 4.0 0.2 HG A:MBO304 0.5 15.8 0.1 HG A:MBO303 0.8 21.5 0.7 CE1 A:MBO303 2.0 15.6 0.7 CE1 A:MBO303 2.2 3.6 0.2 SG A:CYS206 2.5 8.8 0.6 CE2 A:MBO303 2.6 15.8 0.7 O A:GLU205 2.9 9.1 1.0 O A:GLN137 3.0 8.6 1.0 CE2 A:MBO303 3.1 3.7 0.2 CE6 A:MBO303 3.2 16.5 0.7 O A:HOH507 3.2 20.0 1.0 CE6 A:MBO303 3.2 4.6 0.2 CB A:CYS206 3.2 7.3 0.2 CB A:CYS206 3.3 9.3 0.6 C A:GLU205 3.3 7.5 1.0 C A:GLN137 3.3 8.0 1.0 CB A:CYS206 3.4 7.8 0.2 SG A:CYS206 3.4 8.0 0.2 CA A:CYS206 3.5 7.0 0.2 CA A:CYS206 3.5 7.2 0.6 CA A:CYS206 3.5 7.1 0.2 N A:CYS206 3.6 7.3 1.0 N A:GLN137 3.8 8.9 1.0 O A:HOH456 3.8 19.8 1.0 N A:PRO138 3.9 8.2 1.0 CE3 A:MBO303 3.9 19.5 0.7 CA A:PRO138 3.9 8.9 1.0 CA A:GLN137 4.1 8.5 1.0 N A:GLU205 4.2 8.8 1.0 O A:VAL135 4.3 13.7 1.0 C A:GLN136 4.3 10.1 1.0 CA A:GLU205 4.3 8.0 1.0 CE5 A:MBO303 4.4 18.4 0.7 CE3 A:MBO303 4.4 3.7 0.2 CE5 A:MBO303 4.5 4.6 0.2 SG A:CYS206 4.6 8.2 0.2 CE4 A:MBO303 4.6 21.3 0.7 C A:VAL135 4.6 11.5 1.0 O A:GLN136 4.8 12.2 1.0 CA A:GLN136 4.8 10.9 1.0 CD A:PRO138 4.8 10.0 1.0 C A:PRO138 4.9 8.0 1.0 CB A:GLU205 4.9 8.6 1.0 C A:CYS206 4.9 7.0 1.0 C A:LEU204 4.9 7.8 1.0 CE4 A:MBO303 5.0 4.7 0.2 CB A:PRO138 5.0 11.0 1.0

Mercury binding site 3 out of 3 in the Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Structure-Assisted Design of Carborane-Based Inhibitors of Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg304 b:15.8 occ:0.10 HG A:MBO303 0.5 4.0 0.2 HG A:MBO303 1.1 21.5 0.7 CE1 A:MBO303 1.8 15.6 0.7 CE1 A:MBO303 2.0 3.6 0.2 CE2 A:MBO303 2.3 15.8 0.7 SG A:CYS206 2.8 8.8 0.6 CE2 A:MBO303 2.8 3.7 0.2 O A:GLU205 2.9 9.1 1.0 CE6 A:MBO303 2.9 16.5 0.7 O A:HOH507 3.0 20.0 1.0 CE6 A:MBO303 3.0 4.6 0.2 C A:GLU205 3.3 7.5 1.0 O A:HOH456 3.4 19.8 1.0 O A:GLN137 3.4 8.6 1.0 CB A:CYS206 3.6 7.3 0.2 CE3 A:MBO303 3.7 19.5 0.7 CB A:CYS206 3.7 9.3 0.6 SG A:CYS206 3.7 8.0 0.2 C A:GLN137 3.7 8.0 1.0 N A:CYS206 3.8 7.3 1.0 CA A:CYS206 3.8 7.0 0.2 CA A:CYS206 3.8 7.2 0.6 CA A:CYS206 3.8 7.1 0.2 CB A:CYS206 3.8 7.8 0.2 N A:GLU205 4.0 8.8 1.0 CE5 A:MBO303 4.1 18.4 0.7 N A:GLN137 4.1 8.9 1.0 CA A:GLU205 4.1 8.0 1.0 N A:PRO138 4.2 8.2 1.0 CE3 A:MBO303 4.2 3.7 0.2 CA A:PRO138 4.2 8.9 1.0 CE5 A:MBO303 4.3 4.6 0.2 CE4 A:MBO303 4.3 21.3 0.7 O A:VAL135 4.4 13.7 1.0 CA A:GLN137 4.5 8.5 1.0 C A:GLN136 4.5 10.1 1.0 CB A:GLU205 4.6 8.6 1.0 CE4 A:MBO303 4.7 4.7 0.2 C A:LEU204 4.8 7.8 1.0 SG A:CYS206 4.9 8.2 0.2 O A:GLN136 4.9 12.2 1.0 C A:VAL135 4.9 11.5 1.0 CA A:GLN136 5.0 10.9 1.0

P.Mader, A.Pecina, P.Cigler, M.Lepsik, V.Sicha, P.Hobza, B.Gruner, J.Fanfrlik, J.Brynda, P.Rezacova. Carborane-Based Carbonic Anhydrase Inhibitors: Insight Into Caii/Caix Specificity From A High-Resolution Crystal Structure, Modeling, and Quantum Chemical Calculations. Biomed Res Int V.2014 89869 2014.
PubMed: 25309911
DOI: 10.1155/2014/389869