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Fluorine in PDB 3r17: Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide

Enzymatic activity of Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide

All present enzymatic activity of Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide:
4.2.1.1;

Protein crystallography data

The structure of Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide, PDB code: 3r17 was solved by S.Biswas, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.25 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.378, 41.261, 71.943, 90.00, 104.17, 90.00
R / Rfree (%) 15.1 / 19.4

Other elements in 3r17:

The structure of Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide (pdb code 3r17). 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 Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide, PDB code: 3r17:

Fluorine binding site 1 out of 1 in 3r17

Go back to Fluorine Binding Sites List in 3r17
Fluorine binding site 1 out of 1 in the Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Hcarbonic Anhydrase II Bound to N-(2-Fluoro.4-Sulfamoylphenyl)-2- (Thiophen-2-Yl) Acetamide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1

b:16.8
occ:1.00
 F01 B:5UM1 0.0 16.8 1.0
C03 B:5UM1 1.3 15.5 1.0
C02 B:5UM1 2.3 13.6 1.0
C04 B:5UM1 2.3 15.4 1.0
N07 B:5UM1 2.7 15.9 1.0
O1 B:GOL263 3.1 30.1 1.0
NE2 B:GLN92 3.3 13.3 1.0
CZ B:PHE131 3.4 19.3 1.0
C01 B:5UM1 3.6 10.9 1.0
C05 B:5UM1 3.6 14.2 1.0
CG1 B:VAL121 3.7 10.1 1.0
CE1 B:PHE131 3.9 15.5 1.0
C08 B:5UM1 4.1 22.5 1.0
C06 B:5UM1 4.1 12.3 1.0
O3 B:GOL1816 4.2 20.0 1.0
CG2 B:VAL121 4.2 11.0 1.0
C1 B:GOL263 4.3 37.1 1.0
CD B:GLN92 4.4 13.5 1.0
O2 B:GOL263 4.4 46.9 1.0
CB B:VAL121 4.4 9.9 1.0
CD2 B:LEU198 4.5 12.1 1.0
CE2 B:PHE131 4.5 19.9 1.0
CD1 B:LEU141 4.6 11.4 1.0
C3 B:GOL1816 4.7 17.4 1.0
O08 B:5UM1 4.8 21.1 1.0
C09 B:5UM1 4.9 20.3 1.0
CG B:GLN92 5.0 12.6 1.0

Reference:

S.Biswas, M.Aggarwal, O.Guzel, A.Scozzafava, R.Mckenna, C.T.Supuran. Conformational Variability of Different Sulfonamide Inhibitors with Thienyl-Acetamido Moieties Attributes to Differential Binding in the Active Site of Cytosolic Human Carbonic Anhydrase Isoforms. Bioorg.Med.Chem. V. 19 3732 2011.
ISSN: ISSN 0968-0896
PubMed: 21620713
DOI: 10.1016/J.BMC.2011.05.006
Page generated: Wed Jul 31 22:11:26 2024

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