Zinc in PDB 7u5w: Crystal Structure Analysis of Human Carbonic Anhydrase 2

All present enzymatic activity of Crystal Structure Analysis of Human Carbonic Anhydrase 2:
4.2.1.1;

The structure of Crystal Structure Analysis of Human Carbonic Anhydrase 2, PDB code: 7u5w was solved by H.-S.Seo, S.Dhe-Paganon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.61 / 1.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.16, 71.46, 73.82, 90, 90, 90
R / Rfree (%)	15.7 / 18

The structure of Crystal Structure Analysis of Human Carbonic Anhydrase 2 also contains other interesting chemical elements:

Fluorine

(F)

12 atoms

The binding sites of Zinc atom in the Crystal Structure Analysis of Human Carbonic Anhydrase 2 (pdb code 7u5w). 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 Crystal Structure Analysis of Human Carbonic Anhydrase 2, PDB code: 7u5w:

Zinc binding site 1 out of 1 in the Crystal Structure Analysis of Human Carbonic Anhydrase 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Human Carbonic Anhydrase 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.4 occ:1.00 O A:HOH473 1.9 8.9 1.0 NE2 A:HIS94 2.0 8.8 1.0 ND1 A:HIS119 2.0 7.8 1.0 NE2 A:HIS96 2.0 8.2 1.0 CE1 A:HIS119 2.9 8.1 1.0 CD2 A:HIS94 3.0 8.5 1.0 CE1 A:HIS96 3.0 8.5 1.0 CD2 A:HIS96 3.0 8.2 1.0 CE1 A:HIS94 3.1 8.6 1.0 CG A:HIS119 3.2 7.7 1.0 CB A:HIS119 3.6 8.2 1.0 O A:HOH500 3.7 15.2 1.0 OG1 A:THR198 3.8 8.5 1.0 OE1 A:GLU106 4.0 8.6 1.0 O A:HOH579 4.1 14.3 1.0 NE2 A:HIS119 4.1 8.1 1.0 O A:HOH687 4.1 20.7 1.0 CG A:HIS94 4.1 8.8 1.0 ND1 A:HIS94 4.1 8.9 1.0 ND1 A:HIS96 4.1 9.0 1.0 CG A:HIS96 4.2 8.3 1.0 CD2 A:HIS119 4.2 8.6 1.0 O A:HOH699 4.7 21.1 1.0 CD A:GLU106 4.9 8.5 1.0

H.-S.Seo, S.Dhe-Paganon. Crystal Structure Analysis of Human Carbonic Anhydrase 2 To Be Published.