Zinc in PDB 3r16: Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide

All present enzymatic activity of Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide:
4.2.1.1;

The structure of Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide, PDB code: 3r16 was solved by S.Biswas, R.Mckenna, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.40 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.426, 41.388, 72.019, 90.00, 104.13, 90.00
R / Rfree (%)	15.1 / 17.3

The binding sites of Zinc atom in the Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide (pdb code 3r16). 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 Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide, PDB code: 3r16:

Zinc binding site 1 out of 1 in the Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Caii Bound to N-(4-Sulfamoylphenyl)-2-(Thiophen-2-Yl) Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:9.1 occ:1.00 N01 A:5UN1 2.0 7.7 1.0 NE2 A:HIS94 2.0 6.9 1.0 NE2 A:HIS96 2.1 6.6 1.0 ND1 A:HIS119 2.1 7.7 1.0 CE1 A:HIS119 2.9 7.2 1.0 CD2 A:HIS94 3.0 8.6 1.0 CD2 A:HIS96 3.0 7.8 1.0 CE1 A:HIS94 3.0 8.3 1.0 CE1 A:HIS96 3.1 7.0 1.0 S01 A:5UN1 3.1 11.4 1.0 O02 A:5UN1 3.1 10.4 1.0 CG A:HIS119 3.2 6.5 1.0 CB A:HIS119 3.6 6.2 1.0 OG1 A:THR199 3.9 7.5 1.0 OE1 A:GLU106 4.0 9.0 1.0 NE2 A:HIS119 4.1 7.7 1.0 ND1 A:HIS94 4.1 7.9 1.0 CG A:HIS94 4.1 7.9 1.0 O01 A:5UN1 4.1 10.0 1.0 ND1 A:HIS96 4.2 6.7 1.0 CG A:HIS96 4.2 7.4 1.0 C01 A:5UN1 4.2 11.0 1.0 CD2 A:HIS119 4.2 5.9 1.0 C1 A:GOL1816 4.4 10.0 1.0 C02 A:5UN1 4.8 11.5 1.0 CD A:GLU106 4.9 9.8 1.0 C06 A:5UN1 5.0 13.8 1.0

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