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Mercury in PDB 3t5z: Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide

Enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide

All present enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide, PDB code: 3t5z was solved by A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.110, 41.320, 71.840, 90.00, 104.32, 90.00
R / Rfree (%) 17.9 / 21.1

Other elements in 3t5z:

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide 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 Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide (pdb code 3t5z). 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 Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide, PDB code: 3t5z:

Mercury binding site 1 out of 1 in 3t5z

Go back to Mercury Binding Sites List in 3t5z
Mercury binding site 1 out of 1 in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide


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 Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg264

b:17.4
occ:1.00
 HG A:MBO264 0.0 17.4 1.0
CE1 A:MBO264 2.0 19.8 1.0
SG A:CYS206 2.3 16.1 1.0
O A:GLN137 2.9 9.2 1.0
O A:HOH603 2.9 25.1 1.0
CE6 A:MBO264 3.0 20.2 1.0
CE2 A:MBO264 3.0 18.6 1.0
CB A:CYS206 3.2 11.8 1.0
O A:GLU205 3.2 8.4 1.0
C A:GLN137 3.4 8.9 1.0
C A:GLU205 3.5 7.5 1.0
CA A:CYS206 3.6 6.8 1.0
N A:CYS206 3.7 7.9 1.0
O A:VAL135 3.8 12.8 1.0
N A:GLN137 3.8 9.5 1.0
O A:HOH404 3.9 21.3 1.0
N A:PRO138 4.0 8.8 1.0
O A:HOH586 4.1 35.6 1.0
CA A:GLN137 4.1 8.0 1.0
CA A:PRO138 4.1 9.2 1.0
C A:GLN136 4.1 10.7 0.5
C A:GLN136 4.2 10.6 0.5
C A:VAL135 4.3 11.2 1.0
N A:GLU205 4.3 7.8 1.0
CE5 A:MBO264 4.3 21.2 1.0
CE3 A:MBO264 4.3 21.3 1.0
CA A:GLU205 4.5 7.7 1.0
CA A:GLN136 4.5 11.0 0.5
CA A:GLN136 4.6 10.9 0.5
N A:GLN136 4.6 11.0 0.5
N A:GLN136 4.6 11.0 0.5
O A:GLN136 4.7 11.1 0.5
O A:GLN136 4.7 11.1 0.5
O A:HOH464 4.9 28.3 1.0
CE4 A:MBO264 4.9 21.9 1.0
CB A:LEU204 5.0 11.6 1.0
C A:LEU204 5.0 8.9 1.0
C A:PRO138 5.0 7.3 1.0

Reference:

A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone. Carbonic Anhydrase Inhibitors: X-Ray Crystallographic Studies For the Binding of N-Substituted Benzenesulfonamides to Human Isoform II. Chem.Commun.(Camb.) V. 47 11636 2011.
ISSN: ISSN 1359-7345
PubMed: 21952494
DOI: 10.1039/C1CC14575D
Page generated: Sun Dec 13 19:10:25 2020

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