Zinc in PDB 3m1q: Carbonic Anhydrase II Mutant W5C-H64C with Opened Disulfide Bond

All present enzymatic activity of Carbonic Anhydrase II Mutant W5C-H64C with Opened Disulfide Bond:
4.2.1.1;

The structure of Carbonic Anhydrase II Mutant W5C-H64C with Opened Disulfide Bond, PDB code: 3m1q was solved by J.Schulze Wischeler, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.69
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.200, 41.400, 72.000, 90.00, 104.30, 90.00
R / Rfree (%)	16 / 20.9

The binding sites of Zinc atom in the Carbonic Anhydrase II Mutant W5C-H64C with Opened Disulfide Bond (pdb code 3m1q). 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 Mutant W5C-H64C with Opened Disulfide Bond, PDB code: 3m1q:

Zinc binding site 1 out of 1 in the Carbonic Anhydrase II Mutant W5C-H64C with Opened Disulfide Bond


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 W5C-H64C with Opened Disulfide Bond within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:12.5 occ:1.00 NE2 A:HIS94 2.0 11.7 1.0 NE2 A:HIS96 2.1 11.8 1.0 ND1 A:HIS119 2.1 11.8 1.0 O A:HOH1203 2.3 16.9 1.0 CD2 A:HIS94 2.9 10.8 1.0 CE1 A:HIS94 3.0 11.7 1.0 CE1 A:HIS119 3.0 7.9 1.0 CE1 A:HIS96 3.0 14.3 1.0 CD2 A:HIS96 3.1 9.9 1.0 CG A:HIS119 3.2 9.2 1.0 CB A:HIS119 3.6 9.0 1.0 OG1 A:THR199 3.7 13.2 1.0 OE1 A:GLU106 4.1 15.1 1.0 CG A:HIS94 4.1 11.1 1.0 ND1 A:HIS94 4.1 11.7 1.0 ND1 A:HIS96 4.2 14.1 1.0 NE2 A:HIS119 4.2 8.4 1.0 CG A:HIS96 4.2 10.8 1.0 CD2 A:HIS119 4.2 8.8 1.0 O A:HOH1115 4.8 36.6 1.0 CD A:GLU106 4.9 17.8 1.0

J.Schulze Wischeler, N.U.Sandner, A.Heine, G.Klebe. Mutational Study on Carbonic Anhydrase II To Be Published.