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Mercury in PDB 3c7p: Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237

Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237

All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237, PDB code: 3c7p was solved by A.Di Fiore, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.050, 41.440, 71.670, 90.00, 104.35, 90.00
R / Rfree (%) 18.1 / 20.2

Other elements in 3c7p:

The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237 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 of Human Carbonic Anhydrase II in Complex with STX237 (pdb code 3c7p). 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 Human Carbonic Anhydrase II in Complex with STX237, PDB code: 3c7p:

Mercury binding site 1 out of 1 in 3c7p

Go back to Mercury Binding Sites List in 3c7p
Mercury binding site 1 out of 1 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with STX237


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 Human Carbonic Anhydrase II in Complex with STX237 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg266

b:21.5
occ:1.00
 HG A:MBO266 0.0 21.5 1.0
CE1 A:MBO266 2.0 21.4 1.0
SG A:CYS206 2.2 16.1 1.0
O A:GLN137 2.9 9.8 1.0
CE6 A:MBO266 3.0 21.3 1.0
O A:HOH500 3.0 26.3 1.0
CE2 A:MBO266 3.0 21.2 1.0
O A:GLU205 3.0 9.6 1.0
CB A:CYS206 3.1 14.5 1.0
C A:GLU205 3.4 10.4 1.0
C A:GLN137 3.4 10.8 1.0
CA A:CYS206 3.4 11.0 1.0
N A:CYS206 3.6 11.5 1.0
N A:GLN137 3.9 13.0 1.0
N A:PRO138 3.9 10.7 1.0
O A:HOH426 4.0 20.4 1.0
CA A:PRO138 4.1 10.7 1.0
O A:VAL135 4.1 17.5 1.0
CA A:GLN137 4.2 10.2 1.0
C A:GLN136 4.2 15.5 1.0
N A:GLU205 4.3 7.9 1.0
CE5 A:MBO266 4.3 21.4 1.0
CE3 A:MBO266 4.3 21.3 1.0
CA A:GLU205 4.4 8.8 1.0
C A:VAL135 4.5 16.2 1.0
O A:GLN136 4.6 14.9 1.0
CA A:GLN136 4.6 17.4 1.0
N A:GLN136 4.8 17.0 1.0
CE4 A:MBO266 4.9 21.8 1.0
O A:HOH496 4.9 27.6 1.0
CD A:PRO138 4.9 12.8 1.0
C A:CYS206 4.9 10.8 1.0
C A:PRO138 4.9 10.7 1.0
C A:LEU204 5.0 8.6 1.0

Reference:

L.W.L.Woo, D.S.Fischer, C.M.Sharland, M.Trusselle, P.A.Foster, S.K.Chander, A.Di Fiore, C.T.Supuran, G.De Simone, A.Purohit, M.J.Reed, B.V.L.Potter. Anticancer Steroid Sulfatase Inhibitors: Synthesis of A Potent Fluorinated Second-Generation Agent, in Vitro and in Vivo Activities, Molecular Modeling, and Protein Crystallography Mol.Cancer Ther. V. 7 2435 2008.
ISSN: ISSN 1535-7163
PubMed: 18723489
DOI: 10.1158/1535-7163.MCT-08-0195
Page generated: Fri Aug 8 10:05:09 2025

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