Zinc in PDB 8vzg: Carbonic Anhydrase II Mutant with Drd Function

All present enzymatic activity of Carbonic Anhydrase II Mutant with Drd Function:
4.2.1.1; 4.2.1.69;

The structure of Carbonic Anhydrase II Mutant with Drd Function, PDB code: 8vzg was solved by D.K.Sethi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.15 / 1.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.534, 69.042, 80.075, 90, 90, 90
R / Rfree (%)	15 / 18.1

The binding sites of Zinc atom in the Carbonic Anhydrase II Mutant with Drd Function (pdb code 8vzg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Carbonic Anhydrase II Mutant with Drd Function, PDB code: 8vzg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Carbonic Anhydrase II Mutant with Drd Function


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 Mutant with Drd Function within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn306 b:15.9 occ:1.00 N1 A:AZM301 2.0 17.9 1.0 NE2 A:HIS94 2.0 16.1 1.0 ND1 A:HIS119 2.1 15.4 1.0 NE2 A:HIS96 2.1 16.7 1.0 O2 A:AZM301 2.9 16.9 1.0 CE1 A:HIS119 3.0 15.1 1.0 CD2 A:HIS94 3.0 16.4 1.0 CE1 A:HIS94 3.0 16.3 1.0 S1 A:AZM301 3.0 18.6 1.0 CD2 A:HIS96 3.1 16.6 1.0 CE1 A:HIS96 3.1 16.5 1.0 CG A:HIS119 3.1 14.3 1.0 CB A:HIS119 3.6 14.5 1.0 OG1 A:THR198 3.9 15.2 1.0 OE1 A:GLU106 4.0 16.7 1.0 C1 A:AZM301 4.1 15.8 1.0 O1 A:AZM301 4.1 16.5 1.0 ND1 A:HIS94 4.1 16.6 1.0 NE2 A:HIS119 4.1 15.9 1.0 CG A:HIS94 4.2 14.7 1.0 CD2 A:HIS119 4.2 14.7 1.0 CG A:HIS96 4.2 16.0 1.0 ND1 A:HIS96 4.3 17.6 1.0 N3 A:AZM301 4.8 15.3 1.0 C1 A:GOL303 4.9 25.1 1.0 CD A:GLU106 5.0 17.9 1.0

Zinc binding site 2 out of 2 in the Carbonic Anhydrase II Mutant with Drd Function


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Carbonic Anhydrase II Mutant with Drd Function within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn307 b:19.5 occ:1.00 NE2 A:HIS64 2.0 17.4 1.0 NE2 A:HIS4 2.1 19.0 1.0 CE1 A:HIS64 3.0 16.4 1.0 CE1 A:HIS4 3.0 19.3 1.0 CD2 A:HIS64 3.0 17.6 1.0 CD2 A:HIS4 3.0 18.7 1.0 NE1 A:TRP5 3.7 20.1 1.0 O A:HOH512 3.8 22.4 1.0 CE2 A:TRP5 4.0 16.9 1.0 CZ2 A:TRP5 4.1 18.6 1.0 ND1 A:HIS64 4.1 17.7 1.0 ND1 A:HIS4 4.2 19.4 1.0 CG A:HIS64 4.2 16.1 1.0 CG A:HIS4 4.2 17.7 1.0 CD1 A:TRP5 4.5 19.0 1.0 O A:ASN62 4.7 19.1 1.0 CD2 A:TRP5 4.9 17.1 1.0

M.Innis, J.T.Meulen, D.K.Sethi. Functional Regulation of Membrane-Bound Cytokine Activity in Engineered T Cells Via Drug-Responsive Domains Derived From Carbonic Anhydrase 2 To Be Published.