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Mercury in PDB 2nno: Structure of Inhibitor Binding to Carbonic Anhydrase II

Enzymatic activity of Structure of Inhibitor Binding to Carbonic Anhydrase II

All present enzymatic activity of Structure of Inhibitor Binding to Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structure of Inhibitor Binding to Carbonic Anhydrase II, PDB code: 2nno was solved by D.W.Christianson, K.M.Jude, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 1.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.280, 41.361, 72.135, 90.00, 104.50, 90.00
R / Rfree (%) 12.2 / 14.8

Other elements in 2nno:

The structure of Structure of Inhibitor Binding to Carbonic Anhydrase II also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of Inhibitor Binding to Carbonic Anhydrase II (pdb code 2nno). 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 Structure of Inhibitor Binding to Carbonic Anhydrase II, PDB code: 2nno:

Mercury binding site 1 out of 1 in 2nno

Go back to Mercury Binding Sites List in 2nno
Mercury binding site 1 out of 1 in the Structure of Inhibitor Binding to 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 Structure of Inhibitor Binding to Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg206

b:17.1
occ:0.71
HG A:CMH206 0.0 17.1 0.7
CM A:CMH206 2.0 30.7 0.7
SG A:CMH206 2.3 13.0 0.7
O A:HOH563 2.4 55.9 1.0
CB A:CMH206 2.9 10.6 0.3
O A:GLN137 3.0 10.3 1.0
CB A:CMH206 3.2 10.6 0.7
O A:VAL135 3.3 14.8 1.0
O A:GLU205 3.3 9.9 1.0
C A:GLN137 3.5 10.3 1.0
CA A:CMH206 3.5 8.3 1.0
N A:GLN137 3.5 10.7 1.0
C A:GLU205 3.5 8.9 1.0
N A:CMH206 3.7 8.1 1.0
C A:VAL135 3.8 12.2 1.0
C A:GLN136 3.9 11.6 1.0
O A:HOH485 4.0 22.0 1.0
SG A:CMH206 4.1 12.6 0.3
CA A:GLN137 4.1 10.6 1.0
N A:GLU205 4.1 8.5 1.0
N A:PRO138 4.2 10.4 1.0
CA A:GLN136 4.3 12.9 1.0
N A:GLN136 4.3 11.6 1.0
CA A:GLU205 4.4 8.6 1.0
CA A:PRO138 4.4 10.6 1.0
O A:GLN136 4.5 14.7 1.0
CA A:VAL135 4.5 11.7 1.0
O A:HOH430 4.5 17.5 1.0
CB A:LEU204 4.6 10.2 1.0
C A:LEU204 4.7 8.0 1.0
O A:ALA134 4.8 9.9 1.0
O A:HOH677 4.9 34.9 1.0
C A:CMH206 5.0 8.0 1.0

Reference:

D.K.Srivastava, K.M.Jude, A.L.Banerjee, M.Haldar, S.Manokaran, J.Kooren, S.Mallik, D.W.Christianson. Structural Analysis of Charge Discrimination in the Binding of Inhibitors to Human Carbonic Anhydrases I and II. J.Am.Chem.Soc. V. 129 5528 2007.
ISSN: ISSN 0002-7863
PubMed: 17407288
DOI: 10.1021/JA068359W
Page generated: Wed Oct 28 18:41:45 2020

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