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Zinc in PDB 6rqi: Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide

Enzymatic activity of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide

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

Protein crystallography data

The structure of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6rqi 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) 41.02 / 0.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.395, 41.527, 72.256, 90.00, 104.64, 90.00
R / Rfree (%) 11.6 / 13

Other elements in 6rqi:

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

Fluorine (F) 1 atom
Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide (pdb code 6rqi). 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 Fluorinated Benzenesulfonamide, PDB code: 6rqi:

Zinc binding site 1 out of 1 in 6rqi

Go back to Zinc Binding Sites List in 6rqi
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide


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 Fluorinated Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:5.2
occ:1.00
 N2 A:FBW307 2.0 6.0 1.0
NE2 A:HIS94 2.0 5.7 1.0
ND1 A:HIS119 2.0 5.2 1.0
NE2 A:HIS96 2.0 5.5 1.0
CE1 A:HIS119 2.9 5.3 1.0
CD2 A:HIS94 3.0 5.8 1.0
O2 A:FBW307 3.0 6.6 1.0
CD2 A:HIS96 3.0 5.7 1.0
CE1 A:HIS94 3.0 5.8 1.0
HE1 A:HIS119 3.0 6.3 1.0
S A:FBW307 3.0 5.9 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 7.0 1.0
HD2 A:HIS96 3.2 6.9 1.0
HB2 A:HIS119 3.2 6.4 1.0
HE1 A:HIS94 3.2 7.0 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 5.3 1.0
HB3 A:HIS119 3.7 6.4 1.0
O A:HOH563 3.8 14.6 1.0
OG1 A:THR199 3.9 5.6 1.0
OE1 A:GLU106 4.0 6.1 1.0
NE2 A:HIS119 4.1 5.5 1.0
O1 A:FBW307 4.1 6.6 1.0
ND1 A:HIS94 4.1 6.2 1.0
CG A:HIS94 4.1 6.0 1.0
ND1 A:HIS96 4.2 7.1 1.0
CG A:HIS96 4.2 6.0 1.0
CD2 A:HIS119 4.2 5.2 1.0
HH2 A:TRP209 4.2 7.9 1.0
C4 A:FBW307 4.2 7.4 1.0
HG23 A:THR200 4.8 13.1 1.0
O A:HOH590 4.8 28.5 1.0
HE2 A:HIS119 4.8 6.6 1.0
C5 A:FBW307 4.9 9.1 1.0
HD1 A:HIS94 4.9 7.4 1.0
CD A:GLU106 4.9 5.8 1.0
HG11 A:VAL143 4.9 8.2 1.0
HD1 A:HIS96 4.9 8.5 1.0

Reference:

S.Glockner, K.Ngo, B.Wagner, A.Heine, G.Klebe. The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32230853
DOI: 10.3390/BIOM10040509
Page generated: Tue Oct 29 06:41:51 2024

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