Zinc in PDB 3igp: Structure of Inhibitor Binding to Carbonic Anhydrase II

All present enzymatic activity of Structure of Inhibitor Binding to Carbonic Anhydrase II:
4.2.1.1;

The structure of Structure of Inhibitor Binding to Carbonic Anhydrase II, PDB code: 3igp was solved by R.Gitto, S.Agnello, J.Brynda, P.Mader, C.T.Supuran, A.Chimirri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.310, 41.270, 72.040, 90.00, 104.22, 90.00
R / Rfree (%)	15.9 / 19.6

The binding sites of Zinc atom in the Structure of Inhibitor Binding to Carbonic Anhydrase II (pdb code 3igp). 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 Inhibitor Binding to Carbonic Anhydrase II, PDB code: 3igp:

Zinc binding site 1 out of 1 in the Structure of Inhibitor Binding to Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Inhibitor Binding to Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:11.4 occ:1.00 NE2 A:HIS96 2.1 7.1 1.0 NE2 A:HIS94 2.1 8.7 1.0 NAD A:DT7263 2.1 10.9 1.0 ND1 A:HIS119 2.1 8.9 1.0 CE1 A:HIS119 2.9 8.7 1.0 CD2 A:HIS94 3.0 9.4 1.0 OAF A:DT7263 3.0 12.1 1.0 CD2 A:HIS96 3.0 6.1 1.0 CE1 A:HIS96 3.1 7.1 1.0 CE1 A:HIS94 3.1 7.6 1.0 SAS A:DT7263 3.1 10.0 1.0 CG A:HIS119 3.1 7.1 1.0 CB A:HIS119 3.6 8.2 1.0 OG1 A:THR199 3.8 9.5 1.0 OE1 A:GLU106 4.0 7.5 1.0 NE2 A:HIS119 4.1 8.6 1.0 CG A:HIS94 4.2 5.8 1.0 ND1 A:HIS96 4.2 9.4 1.0 ND1 A:HIS94 4.2 7.4 1.0 CG A:HIS96 4.2 8.7 1.0 NAR A:DT7263 4.2 19.3 1.0 CD2 A:HIS119 4.2 7.1 1.0 OAE A:DT7263 4.2 15.8 1.0 C1 A:GOL265 4.6 22.0 1.0 CAQ A:DT7263 4.6 18.0 1.0 CAJ A:DT7263 4.9 20.3 1.0 CD A:GLU106 4.9 10.7 1.0

R.Gitto, S.Agnello, S.Ferro, L.De Luca, D.Vullo, J.Brynda, P.Mader, C.T.Supuran, A.Chimirri. Identification of 3,4-Dihydroisoquinoline-2(1H)-Sulfonamides As Potent Carbonic Anhydrase Inhibitors: Synthesis, Biological Evaluation, and Enzyme-Ligand X-Ray Studies. J.Med.Chem. 2010.
ISSN: ISSN 0022-2623
PubMed: 20170095
DOI: 10.1021/JM9014026