Zinc in PDB 5y2s: 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II

All present enzymatic activity of 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II:
4.2.1.1;

The structure of 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II, PDB code: 5y2s was solved by C.U.Kim, S.Y.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.71 / 0.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.305, 41.365, 71.944, 90.00, 104.12, 90.00
R / Rfree (%)	11.2 / 12.7

The binding sites of Zinc atom in the 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II (pdb code 5y2s). 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 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II, PDB code: 5y2s:

Zinc binding site 1 out of 1 in the 7.0 Atm CO2-Pressurized Human 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 7.0 Atm CO2-Pressurized Human Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:3.6 occ:1.00 O A:HOH455 1.9 7.1 1.0 NE2 A:HIS94 2.0 3.8 1.0 ND1 A:HIS119 2.0 3.5 1.0 NE2 A:HIS96 2.0 3.7 1.0 CE1 A:HIS119 2.9 3.9 1.0 CD2 A:HIS94 2.9 3.9 1.0 CD2 A:HIS96 3.0 3.8 1.0 CE1 A:HIS94 3.0 4.0 1.0 CE1 A:HIS96 3.0 4.6 1.0 CG A:HIS119 3.1 3.5 1.0 O1 A:CO2302 3.3 8.8 1.0 O A:HOH595 3.6 16.0 0.8 CB A:HIS119 3.6 3.4 1.0 C A:CO2302 3.7 8.3 1.0 OG1 A:THR199 3.8 4.2 1.0 OE1 A:GLU106 4.0 4.5 1.0 NE2 A:HIS119 4.1 3.9 1.0 CG A:HIS94 4.1 3.6 1.0 ND1 A:HIS94 4.1 3.9 1.0 ND1 A:HIS96 4.2 5.0 1.0 CG A:HIS96 4.2 3.8 1.0 CD2 A:HIS119 4.2 3.8 1.0 O A:HOH457 4.3 17.8 1.0 O A:HOH728 4.4 15.1 1.0 O2 A:CO2302 4.4 11.4 1.0 CD A:GLU106 4.9 3.9 1.0

J.K.Kim, C.L.Lomelino, B.S.Avvaru, B.P.Mahon, R.Mckenna, S.Park, C.U.Kim. Active-Site Solvent Replenishment Observed During Human Carbonic Anhydrase II Catalysis. Iucrj V. 5 93 2018.
ISSN: ESSN 2052-2525
PubMed: 29354275
DOI: 10.1107/S2052252517017626