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Fluorine 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:

Mercury (Hg) 2 atoms
Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine 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 Fluorine atom.
In total only one binding site of Fluorine was determined in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6rqi:

Fluorine binding site 1 out of 1 in 6rqi

Go back to Fluorine Binding Sites List in 6rqi
Fluorine 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 Fluorine with other atoms in the F 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:F307

b:12.1
occ:1.00
 F A:FBW307 0.0 12.1 1.0
C2 A:FBW307 1.4 9.7 1.0
C1 A:FBW307 2.3 10.4 1.0
C3 A:FBW307 2.4 8.6 1.0
HG11 A:VAL121 2.5 8.2 1.0
HZ A:PHE131 2.9 14.6 1.0
HE21 A:GLN92 3.1 11.4 1.0
HG21 A:VAL121 3.4 7.7 1.0
HE1 A:PHE131 3.4 13.4 1.0
CG1 A:VAL121 3.4 6.8 1.0
NE2 A:GLN92 3.5 9.5 1.0
C6 A:FBW307 3.6 10.5 1.0
CZ A:PHE131 3.6 12.2 1.0
C4 A:FBW307 3.6 7.4 1.0
HE22 A:GLN92 3.6 11.4 1.0
HG13 A:VAL121 3.7 8.2 1.0
HD22 A:LEU198 3.7 10.6 1.0
CE1 A:PHE131 3.8 11.2 1.0
HG12 A:VAL121 4.0 8.2 1.0
C5 A:FBW307 4.1 9.1 1.0
CG2 A:VAL121 4.1 6.5 1.0
HD21 A:LEU198 4.2 10.6 1.0
HD13 A:LEU141 4.3 10.8 1.0
CB A:VAL121 4.3 6.0 1.0
HG22 A:VAL121 4.3 7.7 1.0
CD2 A:LEU198 4.4 8.8 1.0
O A:HOH556 4.4 20.1 1.0
HB A:VAL121 4.4 7.2 1.0
CD A:GLN92 4.5 7.0 1.0
HE1 A:HIS94 4.7 7.0 1.0
HD11 A:LEU141 4.7 10.8 1.0
HG3 A:GLN92 4.7 9.4 1.0
CE2 A:PHE131 4.8 12.7 1.0
HG2 A:GLN92 4.8 9.4 1.0
O A:HOH577 4.9 32.9 1.0
HD23 A:LEU198 4.9 10.6 1.0
HG23 A:VAL121 4.9 7.7 1.0
HD13 A:LEU198 4.9 11.2 1.0
CD1 A:LEU141 4.9 9.0 1.0
CG A:GLN92 5.0 7.8 1.0
HE2 A:PHE131 5.0 15.3 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: Fri Aug 2 01:20:02 2024

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