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Mercury in PDB 4q8z: Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II

Enzymatic activity of Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II, PDB code: 4q8z was solved by D.P.Martin, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.94 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.212, 41.201, 71.724, 90.00, 104.09, 90.00
R / Rfree (%) 15.3 / 17.7

Other elements in 4q8z:

The structure of Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II (pdb code 4q8z). 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 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II, PDB code: 4q8z:

Mercury binding site 1 out of 1 in 4q8z

Go back to Mercury Binding Sites List in 4q8z
Mercury binding site 1 out of 1 in the Crystal Structure of 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II


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 1-Hydroxy-4-Methylpyridin-2(1H)-One Bound to Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:11.2
occ:1.00
 HG A:MBO302 0.0 11.2 1.0
CE1 A:MBO302 2.2 13.1 1.0
SG A:CYS206 2.3 8.1 1.0
O A:VAL135 3.0 10.9 1.0
CE2 A:MBO302 3.0 15.2 1.0
O A:GLN137 3.0 7.7 1.0
CE6 A:MBO302 3.2 9.2 1.0
CB A:CYS206 3.3 4.5 1.0
CA A:CYS206 3.5 4.9 1.0
C A:VAL135 3.6 6.0 1.0
N A:GLN137 3.6 7.3 1.0
C A:GLN137 3.6 5.9 1.0
N A:CYS206 3.7 5.0 1.0
O A:GLU205 3.7 6.9 1.0
C A:GLU205 3.7 5.7 1.0
N A:GLU205 4.0 7.4 1.0
O A:HOH422 4.0 18.4 1.0
CB A:LEU204 4.1 8.2 1.0
C A:GLN136 4.1 9.4 1.0
CA A:VAL135 4.2 8.1 1.0
CA A:GLN137 4.2 7.4 1.0
N A:GLN136 4.3 7.7 1.0
CE3 A:MBO302 4.3 15.7 1.0
CA A:GLN136 4.4 8.9 1.0
N A:PRO138 4.4 6.5 1.0
C A:LEU204 4.4 7.1 1.0
CA A:GLU205 4.5 5.6 1.0
CE5 A:MBO302 4.5 14.7 1.0
CA A:PRO138 4.6 7.1 1.0
O A:ALA134 4.7 7.2 1.0
CA A:LEU204 4.8 7.2 1.0
O A:GLN136 4.9 10.6 1.0
CE4 A:MBO302 4.9 16.7 1.0
C A:CYS206 5.0 4.2 1.0
CG A:LEU204 5.0 10.7 1.0

Reference:

D.P.Martin, P.G.Blachly, J.A.Mccammon, S.M.Cohen. Exploring the Influence of the Protein Environment on Metal-Binding Pharmacophores. J.Med.Chem. V. 57 7126 2014.
ISSN: ISSN 0022-2623
PubMed: 25116076
DOI: 10.1021/JM500984B
Page generated: Sun Aug 11 05:27:24 2024

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