Zinc in PDB 4iwz: Structure of Hcaii in Complex with An Acetazolamide Derivative

All present enzymatic activity of Structure of Hcaii in Complex with An Acetazolamide Derivative:
4.2.1.1;

The structure of Structure of Hcaii in Complex with An Acetazolamide Derivative, PDB code: 4iwz 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)	24.54 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.242, 41.324, 71.980, 90.00, 104.18, 90.00
R / Rfree (%)	15.2 / 18.5

The binding sites of Zinc atom in the Structure of Hcaii in Complex with An Acetazolamide Derivative (pdb code 4iwz). 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 Structure of Hcaii in Complex with An Acetazolamide Derivative, PDB code: 4iwz:

Zinc binding site 1 out of 1 in the Structure of Hcaii in Complex with An Acetazolamide Derivative


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Hcaii in Complex with An Acetazolamide Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:12.8 occ:0.74 N01 A:1GO301 1.9 17.1 1.0 NE2 A:HIS94 2.0 15.0 1.0 NE2 A:HIS96 2.0 14.7 1.0 ND1 A:HIS119 2.1 15.6 1.0 CD2 A:HIS94 2.9 16.5 1.0 CE1 A:HIS119 3.0 14.2 1.0 CE1 A:HIS94 3.0 15.8 1.0 CD2 A:HIS96 3.0 15.9 1.0 CE1 A:HIS96 3.0 15.0 1.0 S02 A:1GO301 3.0 16.6 1.0 O04 A:1GO301 3.1 16.9 1.0 CG A:HIS119 3.2 14.4 1.0 CB A:HIS119 3.6 14.4 1.0 OG1 A:THR199 3.9 16.5 1.0 OE1 A:GLU106 4.0 15.9 1.0 ND1 A:HIS94 4.1 16.0 1.0 CG A:HIS94 4.1 15.3 1.0 O03 A:1GO301 4.1 18.0 1.0 ND1 A:HIS96 4.1 14.3 1.0 NE2 A:HIS119 4.1 14.6 1.0 CG A:HIS96 4.1 15.0 1.0 C05 A:1GO301 4.2 18.0 1.0 CD2 A:HIS119 4.2 15.9 1.0 C1 A:GOL303 4.5 21.4 1.0 CD A:GLU106 4.9 15.3 1.0 N06 A:1GO301 4.9 20.2 1.0

S.Biswas, R.Mckenna, C.T.Supuran. Effect of Incorporating A Thiophene Tail in the Scaffold of Acetazolamide on the Inhibition of Human Carbonic Anhydrase Isoforms I, II, IX and XII. Bioorg.Med.Chem.Lett. V. 23 5646 2013.
ISSN: ISSN 0960-894X
PubMed: 23993330
DOI: 10.1016/J.BMCL.2013.08.019