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Mercury in PDB 3m14: Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor

Enzymatic activity of Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor

All present enzymatic activity of Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor, PDB code: 3m14 was solved by J.Schulze Wischeler, A.Heine, G.Klebe, N.U.Sandner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.38
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.138, 41.349, 72.033, 90.00, 104.30, 90.00
R / Rfree (%) 12.7 / 17.6

Other elements in 3m14:

The structure of Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor (pdb code 3m14). 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 Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor, PDB code: 3m14:

Mercury binding site 1 out of 1 in 3m14

Go back to Mercury Binding Sites List in 3m14
Mercury binding site 1 out of 1 in the Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II in Complex with Novel Sulfonamide Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg503

b:16.9
occ:0.78
HG A:BE7503 0.0 16.9 0.8
SG A:CYS206 1.6 13.9 0.8
C5 A:BE7503 2.0 10.3 0.8
CB A:CYS206 2.7 27.2 0.8
O A:GLN137 3.0 11.2 1.0
C6 A:BE7503 3.0 16.6 0.8
C4 A:BE7503 3.0 17.4 0.8
O A:GLU205 3.1 11.4 1.0
C A:GLN137 3.4 10.1 1.0
C A:GLU205 3.4 9.4 1.0
CA A:CYS206 3.4 9.1 0.8
CB A:CYS206 3.5 0.0 0.2
CA A:CYS206 3.5 8.5 0.2
N A:CYS206 3.7 8.8 1.0
N A:GLN137 3.7 13.2 1.0
O A:HOH1079 3.9 21.0 1.0
N A:PRO138 3.9 11.1 1.0
CA A:PRO138 4.0 12.0 1.0
O A:VAL135 4.0 19.5 1.0
CA A:GLN137 4.1 11.4 1.0
C A:GLN136 4.1 15.0 1.0
N A:GLU205 4.3 10.6 1.0
C7 A:BE7503 4.3 17.4 0.8
C3 A:BE7503 4.3 18.9 0.8
CA A:GLU205 4.4 9.4 1.0
SG A:CYS206 4.5 14.8 0.2
C A:VAL135 4.5 12.6 1.0
CA A:GLN136 4.6 15.9 1.0
O A:GLN136 4.7 16.8 1.0
N A:GLN136 4.8 14.4 1.0
C2 A:BE7503 4.9 17.9 0.8
C A:CYS206 4.9 9.7 1.0
C A:LEU204 4.9 8.9 1.0
CB A:LEU204 5.0 11.6 1.0
C A:PRO138 5.0 11.1 1.0

Reference:

J.Schulze Wischeler, N.U.Sandner, M.Haake, C.Supuran, A.Heine, G.Klebe. Structural Investigation and Inhibitor Studies on Carbonic Anhydrase II To Be Published.
Page generated: Sun Dec 13 19:10:03 2020

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