Zinc in PDB 6nj3: Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233

All present enzymatic activity of Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233:
4.2.1.1;

The structure of Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233, PDB code: 6nj3 was solved by K.M.Kean, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.55 / 1.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.144, 69.083, 81.106, 90.00, 90.00, 90.00
R / Rfree (%)	10 / 12.5

The binding sites of Zinc atom in the Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233 (pdb code 6nj3). 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 Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233, PDB code: 6nj3:

Zinc binding site 1 out of 1 in the Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermostable Variant of Human Carbonic Anhydrase with Ordered Tetrazine 2.0 at Site 233 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:9.2 occ:0.65 ND1 A:HIS118 2.0 9.2 1.0 NE2 A:HIS93 2.0 9.7 1.0 NE2 A:HIS95 2.1 9.6 1.0 O A:HOH442 2.1 11.6 0.7 O A:ACT301 2.2 12.2 0.7 CE1 A:HIS118 2.9 9.3 1.0 CE1 A:HIS93 3.0 9.2 1.0 HE1 A:HIS118 3.0 11.2 1.0 CD2 A:HIS93 3.1 8.9 1.0 CE1 A:HIS95 3.1 10.1 1.0 CD2 A:HIS95 3.1 9.2 1.0 CG A:HIS118 3.1 7.9 1.0 HE1 A:HIS93 3.1 11.1 1.0 C A:ACT301 3.2 10.9 0.7 HB2 A:HIS118 3.2 9.0 1.0 HE1 A:HIS95 3.2 12.2 1.0 HD2 A:HIS93 3.3 10.7 1.0 HD2 A:HIS95 3.3 11.1 1.0 HG1 A:THR198 3.4 11.8 1.0 O A:HOH588 3.4 20.8 0.3 CB A:HIS118 3.6 7.5 1.0 OXT A:ACT301 3.6 12.6 0.7 OG1 A:THR198 3.7 9.8 1.0 HB3 A:HIS118 3.8 9.0 1.0 OE1 A:GLU105 4.0 10.4 1.0 NE2 A:HIS118 4.0 9.4 1.0 O A:HOH706 4.1 27.4 1.0 ND1 A:HIS93 4.1 9.1 1.0 CD2 A:HIS118 4.2 8.2 1.0 CG A:HIS93 4.2 8.1 1.0 HH2 A:TRP208 4.2 11.5 1.0 ND1 A:HIS95 4.2 10.6 1.0 CG A:HIS95 4.3 8.6 1.0 CH3 A:ACT301 4.5 14.5 0.7 H2 A:ACT301 4.6 17.4 0.7 HE2 A:HIS118 4.8 11.3 1.0 H A:THR198 4.8 10.7 1.0 HD1 A:HIS93 4.9 10.9 1.0 HG23 A:THR199 4.9 15.2 1.0 CD A:GLU105 4.9 9.0 1.0 HG23 A:THR198 5.0 12.2 1.0 HD1 A:HIS95 5.0 12.8 1.0 CB A:THR198 5.0 9.0 1.0

R.M.Bednar, T.W.Golbek, K.M.Kean, W.J.Brown, S.Jana, J.E.Baio, P.A.Karplus, R.A.Mehl. Immobilization of Proteins with Controlled Load and Orientation. Acs Appl Mater Interfaces V. 11 36391 2019.
ISSN: ISSN 1944-8252
PubMed: 31525993
DOI: 10.1021/ACSAMI.9B12746