Zinc in PDB 6klz: Human Carbonic Anhydrase II V143I Variant 00 Atm CO2

All present enzymatic activity of Human Carbonic Anhydrase II V143I Variant 00 Atm CO2:
4.2.1.1;

The structure of Human Carbonic Anhydrase II V143I Variant 00 Atm CO2, PDB code: 6klz was solved by C.U.Kim, J.K.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.06 / 0.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.209, 41.316, 72.177, 90.00, 104.39, 90.00
R / Rfree (%)	10.8 / 12.1

The binding sites of Zinc atom in the Human Carbonic Anhydrase II V143I Variant 00 Atm CO2 (pdb code 6klz). 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 Human Carbonic Anhydrase II V143I Variant 00 Atm CO2, PDB code: 6klz:

Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II V143I Variant 00 Atm CO2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II V143I Variant 00 Atm CO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:3.9 occ:1.00 HE2 A:HIS94 1.2 3.7 1.0 HE2 A:HIS96 1.2 4.0 1.0 HD1 A:HIS119 1.2 4.1 1.0 O A:HOH412 1.9 4.4 0.8 O3 A:BCT303 2.0 5.0 0.2 NE2 A:HIS94 2.0 4.0 1.0 ND1 A:HIS119 2.0 4.1 1.0 NE2 A:HIS96 2.0 4.0 1.0 HO3 A:BCT303 2.6 5.0 0.0 CE1 A:HIS119 2.9 4.0 1.0 CD2 A:HIS94 3.0 4.3 1.0 CE1 A:HIS96 3.0 5.1 1.0 CD2 A:HIS96 3.0 4.3 1.0 CE1 A:HIS94 3.0 4.4 1.0 HE1 A:HIS119 3.0 4.0 1.0 C A:BCT303 3.1 7.7 0.2 CG A:HIS119 3.1 3.8 1.0 HD2 A:HIS94 3.1 4.2 1.0 O1 A:BCT303 3.2 7.7 0.2 HE1 A:HIS96 3.2 5.0 1.0 HD2 A:HIS96 3.2 4.3 1.0 HB2 A:HIS119 3.2 4.0 1.0 HE1 A:HIS94 3.2 4.5 1.0 HG1 A:THR199 3.5 4.5 0.0 CB A:HIS119 3.6 3.9 1.0 O A:HOH514 3.7 6.8 0.8 HB3 A:HIS119 3.8 3.9 1.0 OG1 A:THR199 3.8 4.5 1.0 OE1 A:GLU106 4.0 4.5 1.0 O A:HOH401 4.1 8.1 0.8 NE2 A:HIS119 4.1 4.2 1.0 ND1 A:HIS94 4.1 4.6 1.0 ND1 A:HIS96 4.1 5.5 1.0 CG A:HIS94 4.1 4.3 1.0 O A:HOH403 4.2 7.3 0.2 CG A:HIS96 4.2 4.3 1.0 CD2 A:HIS119 4.2 4.0 1.0 HH2 A:TRP209 4.3 5.3 1.0 O2 A:BCT303 4.3 5.2 0.2 O A:HOH676 4.3 12.7 1.0 O A:HOH402 4.4 15.2 0.8 HG23 A:THR200 4.8 7.4 1.0 HE2 A:HIS119 4.9 4.0 1.0 CD A:GLU106 4.9 4.2 1.0 HD1 A:HIS96 4.9 5.0 1.0 HD1 A:HIS94 4.9 4.3 1.0 H A:THR199 4.9 4.5 1.0

J.K.Kim, C.Lee, S.W.Lim, J.T.Andring, A.Adhikari, R.Mckenna, C.U.Kim. Structural Insights Into the Effect of Active-Site Mutation on the Catalytic Mechanism of Carbonic Anhydrase. Iucrj V. 7 985 2020.
ISSN: ESSN 2052-2525
PubMed: 33209313
DOI: 10.1107/S2052252520011008