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Mercury in PDB 2hl4: Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative

Enzymatic activity of Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative

All present enzymatic activity of Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative, PDB code: 2hl4 was solved by A.Di Fiore, C.T.Supuran, J.-Y.Winum, J.-L.Montero, C.Pedone, A.Scozzafava, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.070, 41.120, 72.060, 90.00, 104.51, 90.00
R / Rfree (%) 17.6 / 19.8

Other elements in 2hl4:

The structure of Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative (pdb code 2hl4). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative, PDB code: 2hl4:

Mercury binding site 1 out of 1 in 2hl4

Go back to Mercury Binding Sites List in 2hl4
Mercury binding site 1 out of 1 in the Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure Analysis of Human Carbonic Anhydrase II in Complex with A Benzenesulfonamide Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg266

b:13.1
occ:1.00
 HG A:MBO266 0.0 13.1 1.0
CE1 A:MBO266 2.0 12.8 1.0
SG A:CYS206 2.3 11.1 1.0
O A:GLN137 2.9 10.6 1.0
O A:HOH444 2.9 17.2 1.0
CE6 A:MBO266 3.0 12.3 1.0
CE2 A:MBO266 3.0 14.3 1.0
O A:GLU205 3.0 7.0 1.0
CB A:CYS206 3.2 10.3 1.0
C A:GLU205 3.4 6.3 1.0
C A:GLN137 3.4 10.1 1.0
CA A:CYS206 3.5 6.3 1.0
N A:CYS206 3.6 6.8 1.0
O A:HOH349 3.8 11.9 1.0
N A:GLN137 3.9 11.7 1.0
N A:PRO138 4.0 9.6 1.0
O A:VAL135 4.1 13.4 1.0
CA A:PRO138 4.2 10.4 1.0
CA A:GLN137 4.2 9.6 1.0
C A:GLN136 4.3 12.8 1.0
N A:GLU205 4.3 6.0 1.0
CE5 A:MBO266 4.3 13.1 1.0
CE3 A:MBO266 4.3 14.5 1.0
CA A:GLU205 4.4 6.1 1.0
C A:VAL135 4.4 11.9 1.0
N A:GLN136 4.7 12.2 1.0
CA A:GLN136 4.7 12.8 1.0
O A:GLN136 4.9 11.7 1.0
CE4 A:MBO266 4.9 14.5 1.0
O A:HOH469 4.9 26.9 1.0
C A:CYS206 5.0 6.4 1.0
CB A:GLU205 5.0 7.5 1.0
C A:LEU204 5.0 6.2 1.0
C A:PRO138 5.0 9.1 1.0

Reference:

A.Di Fiore, A.Scozzafava, J.-Y.Winum, J.-L.Montero, C.Pedone, C.T.Supuran, G.De Simone. Carbonic Anhydrase Inhibitors: Binding of An Antiglaucoma Glycosyl-Sulfanilamide Derivative to Human Isoform II and Its Consequences For the Drug Design of Enzyme Inhibitors Incorporating Sugar Moieties Bioorg.Med.Chem.Lett. V. 17 1726 2007.
ISSN: ISSN 0960-894X
PubMed: 17251017
DOI: 10.1016/J.BMCL.2006.12.099
Page generated: Fri Aug 8 09:50:43 2025

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