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Mercury in PDB 2o4z: Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor

Enzymatic activity of Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor

All present enzymatic activity of Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor, PDB code: 2o4z was solved by C.Temperini, J.Y.Winum, J.L.Montero, A.Scozzafava, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.100, 41.390, 72.300, 90.00, 104.38, 90.00
R / Rfree (%) 20.8 / 26.6

Other elements in 2o4z:

The structure of Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor (pdb code 2o4z). 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 of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor, PDB code: 2o4z:

Mercury binding site 1 out of 1 in 2o4z

Go back to Mercury Binding Sites List in 2o4z
Mercury binding site 1 out of 1 in the Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the Carbonic Anhydrase II Complexed with Hydroxysulfamide Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:31.7
occ:1.00
 CB A:CYS206 3.0 12.9 1.0
O A:GLN137 3.0 14.6 1.0
O A:GLU205 3.3 11.6 1.0
C A:GLN137 3.4 14.3 1.0
CA A:CYS206 3.4 12.5 1.0
C A:GLU205 3.5 11.0 1.0
O A:HOH319 3.5 13.9 1.0
N A:GLN137 3.6 15.8 1.0
N A:CYS206 3.6 11.1 1.0
O A:HOH374 3.9 16.9 1.0
N A:PRO138 3.9 13.9 1.0
CA A:GLN137 4.0 14.9 1.0
C A:GLN136 4.0 16.3 1.0
O A:VAL135 4.1 15.0 1.0
N A:GLU205 4.2 11.4 1.0
CA A:PRO138 4.2 13.1 1.0
SG A:CYS206 4.2 24.2 1.0
O A:HOH433 4.3 30.1 1.0
CA A:GLU205 4.4 11.1 1.0
C A:VAL135 4.4 14.9 1.0
O A:GLN136 4.5 16.3 1.0
CA A:GLN136 4.6 16.4 1.0
N A:GLN136 4.7 15.2 1.0
C A:LEU204 4.8 11.5 1.0
CB A:LEU204 4.9 11.5 1.0
C A:CYS206 4.9 10.8 1.0
CD A:PRO138 4.9 13.8 1.0

Reference:

C.Temperini, J.Y.Winum, J.L.Montero, A.Scozzafava, C.T.Supuran. Carbonic Anhydrase Inhibitors: the X-Ray Crystal Structure of the Adduct of N-Hydroxysulfamide with Isozyme II Explains Why This New Zinc Binding Function Is Effective in the Design of Potent Inhibitors. Bioorg.Med.Chem.Lett. V. 17 2795 2007.
ISSN: ISSN 0960-894X
PubMed: 17346964
DOI: 10.1016/J.BMCL.2007.02.068
Page generated: Sun Dec 13 19:07:42 2020

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