Zinc in PDB 6vj3: Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor

All present enzymatic activity of Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor:
4.2.1.1;

The structure of Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor, PDB code: 6vj3 was solved by C.L.Lomelino, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.15 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.524, 41.399, 72.158, 90.00, 104.44, 90.00
R / Rfree (%)	15.1 / 17.3

The binding sites of Zinc atom in the Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor (pdb code 6vj3). 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 Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor, PDB code: 6vj3:

Zinc binding site 1 out of 1 in the Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase II in Complex with Pyrimidine-Based Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.9 occ:1.00 H222 A:QYA302 1.9 10.9 0.6 H222 A:QYA302 1.9 10.1 0.4 N22 A:QYA302 1.9 9.1 0.6 N22 A:QYA302 2.0 8.4 0.4 H221 A:QYA302 2.0 10.9 0.6 H221 A:QYA302 2.0 10.1 0.4 NE2 A:HIS94 2.0 7.5 1.0 NE2 A:HIS96 2.0 8.5 1.0 ND1 A:HIS119 2.1 8.5 1.0 CE1 A:HIS119 2.9 7.5 1.0 CD2 A:HIS94 3.0 9.7 1.0 CD2 A:HIS96 3.0 8.2 1.0 CE1 A:HIS96 3.0 9.4 1.0 CE1 A:HIS94 3.0 9.1 1.0 S19 A:QYA302 3.1 12.9 0.6 HE1 A:HIS119 3.1 9.0 1.0 S19 A:QYA302 3.1 15.1 0.4 O20 A:QYA302 3.1 13.5 0.6 O20 A:QYA302 3.1 14.3 0.4 HD2 A:HIS94 3.1 11.6 1.0 CG A:HIS119 3.2 7.6 1.0 HD2 A:HIS96 3.2 9.9 1.0 HE1 A:HIS96 3.2 11.3 1.0 HE1 A:HIS94 3.2 11.0 1.0 HB2 A:HIS119 3.3 9.1 1.0 HG1 A:THR199 3.5 10.9 1.0 H32 A:GOL303 3.5 18.0 1.0 CB A:HIS119 3.6 7.6 1.0 O A:HOH439 3.6 21.7 1.0 HB3 A:HIS119 3.8 9.1 1.0 OG1 A:THR199 3.9 9.1 1.0 OE1 A:GLU106 4.0 10.0 1.0 NE2 A:HIS119 4.1 9.1 1.0 ND1 A:HIS94 4.1 8.3 1.0 CG A:HIS94 4.1 7.8 1.0 O21 A:QYA302 4.1 14.1 0.6 ND1 A:HIS96 4.2 9.9 1.0 O21 A:QYA302 4.2 12.3 0.4 CG A:HIS96 4.2 8.1 1.0 C06 A:QYA302 4.2 17.3 0.6 CD2 A:HIS119 4.2 7.3 1.0 C06 A:QYA302 4.3 17.6 0.4 HH2 A:TRP209 4.3 11.1 1.0 H2 A:GOL303 4.3 27.1 1.0 C3 A:GOL303 4.5 15.0 1.0 H31 A:GOL303 4.6 18.0 1.0 H051 A:QYA302 4.8 24.3 0.4 H011 A:QYA302 4.8 24.4 0.6 HE2 A:HIS119 4.9 10.9 1.0 H051 A:QYA302 4.9 24.3 0.6 C05 A:QYA302 4.9 20.2 0.4 HD1 A:HIS94 4.9 10.0 1.0 C01 A:QYA302 4.9 20.4 0.6 HG23 A:THR200 4.9 13.5 1.0 CD A:GLU106 4.9 11.4 1.0 HD1 A:HIS96 4.9 11.8 1.0 C2 A:GOL303 4.9 22.6 1.0 H011 A:QYA302 5.0 24.1 0.4 C05 A:QYA302 5.0 20.2 0.6 HG11 A:VAL143 5.0 12.6 1.0

A.Petreni, A.Bonardi, C.Lomelino, S.M.Osman, Z.A.Alothman, W.M.Eldehna, R.El-Haggar, R.Mckenna, A.Nocentini, C.T.Supuran. Inclusion of A 5-Fluorouracil Moiety in Nitrogenous Bases Derivatives As Human Carbonic Anhydrase IX and XII Inhibitors Produced A Targeted Action Against Mda-Mb-231 and T47D Breast Cancer Cells. Eur.J.Med.Chem. V. 190 12112 2020.
ISSN: ISSN 0223-5234
PubMed: 32044580
DOI: 10.1016/J.EJMECH.2020.112112