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Zinc in PDB 5ll8: Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.

Enzymatic activity of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor., PDB code: 5ll8 was solved by S.Gloeckner, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.98 / 1.03
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.280, 41.450, 71.980, 90.00, 104.22, 90.00
R / Rfree (%) 12 / 14.3

Other elements in 5ll8:

The structure of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor. also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor. (pdb code 5ll8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor., PDB code: 5ll8:

Zinc binding site 1 out of 1 in 5ll8

Go back to Zinc Binding Sites List in 5ll8
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II in Complex with Aliphatic Benzenesulfonamide Inhibitor. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn305

b:5.7
occ:1.00
 N A:6YP306 2.0 6.2 1.0
NE2 A:HIS94 2.0 5.9 1.0
ND1 A:HIS119 2.0 5.3 1.0
NE2 A:HIS96 2.0 5.9 1.0
CE1 A:HIS119 2.9 5.3 1.0
CD2 A:HIS94 3.0 6.1 1.0
CD2 A:HIS96 3.0 6.0 1.0
S A:6YP306 3.0 6.4 1.0
O A:6YP306 3.0 7.0 1.0
HE1 A:HIS119 3.0 6.4 1.0
CE1 A:HIS94 3.0 5.5 1.0
CE1 A:HIS96 3.1 6.8 1.0
CG A:HIS119 3.1 5.3 1.0
HD2 A:HIS94 3.2 7.4 1.0
HD2 A:HIS96 3.2 7.2 1.0
HB2 A:HIS119 3.2 6.1 1.0
HE1 A:HIS94 3.3 6.6 1.0
HE1 A:HIS96 3.3 8.1 1.0
HG1 A:THR199 3.5 6.8 1.0
CB A:HIS119 3.6 5.1 1.0
HB3 A:HIS119 3.7 6.1 1.0
OG1 A:THR199 3.9 5.7 1.0
OE1 A:GLU106 4.0 6.1 1.0
NE2 A:HIS119 4.1 5.7 1.0
O1 A:6YP306 4.1 6.7 1.0
C7 A:6YP306 4.1 7.5 1.0
ND1 A:HIS94 4.1 6.0 1.0
CG A:HIS94 4.2 6.0 1.0
ND1 A:HIS96 4.2 7.0 1.0
CG A:HIS96 4.2 6.0 1.0
HH2 A:TRP209 4.2 8.0 1.0
CD2 A:HIS119 4.2 5.6 1.0
C3 A:GOL301 4.5 10.3 1.0
HG23 A:THR200 4.7 9.7 1.0
C8 A:6YP306 4.8 8.1 1.0
HE2 A:HIS119 4.8 6.9 1.0
C6 A:6YP306 4.9 8.8 1.0
HD1 A:HIS94 4.9 7.2 1.0
CD A:GLU106 4.9 6.2 1.0
HG11 A:VAL143 4.9 7.8 1.0
HD1 A:HIS96 5.0 8.3 1.0

Reference:

S.Gloeckner, A.Heine, G.Klebe. Crystallographic, Kinetic and Thermodynamic Characterization of Aliphatic Benzenesulfonamides As Ligands of Human Carbonic Anhydrase II To Be Published.
Page generated: Sun Oct 27 21:06:46 2024

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