Zinc in PDB 6nj6: Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo

All present enzymatic activity of Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo:
4.2.1.1;

The structure of Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo, PDB code: 6nj6 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)	54.76 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.330, 93.860, 100.380, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.3

The binding sites of Zinc atom in the Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo (pdb code 6nj6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo, PDB code: 6nj6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo


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 Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn306 b:16.5 occ:1.00 O4 A:SO4307 1.9 23.0 0.7 O A:HOH407 1.9 21.1 0.3 NE2 A:HIS93 2.0 15.7 1.0 ND1 A:HIS118 2.0 15.5 1.0 NE2 A:HIS95 2.1 15.5 1.0 O3 A:SO4307 2.8 24.5 0.7 S A:SO4307 2.8 24.9 0.7 CE1 A:HIS118 2.9 15.2 1.0 CD2 A:HIS93 3.0 15.6 1.0 CD2 A:HIS95 3.0 15.6 1.0 CE1 A:HIS93 3.1 16.1 1.0 HE1 A:HIS118 3.1 18.3 1.0 CE1 A:HIS95 3.1 16.0 1.0 HD2 A:HIS93 3.1 18.8 1.0 CG A:HIS118 3.1 14.8 1.0 HB2 A:HIS118 3.1 17.7 1.0 HD2 A:HIS95 3.1 18.7 1.0 HE1 A:HIS93 3.3 19.4 1.0 HE1 A:HIS95 3.3 19.1 1.0 CB A:HIS118 3.5 14.7 1.0 HG1 A:THR198 3.6 18.9 1.0 O2 A:SO4307 3.7 28.2 0.7 HB3 A:HIS118 3.7 17.7 1.0 O A:HOH641 3.8 42.1 1.0 O A:HOH595 3.8 28.3 0.3 OG1 A:THR198 3.9 15.8 1.0 O1 A:SO4307 3.9 23.4 0.7 OE1 A:GLU105 4.1 16.1 1.0 NE2 A:HIS118 4.1 15.2 1.0 CG A:HIS93 4.1 16.0 1.0 ND1 A:HIS93 4.1 16.2 1.0 CG A:HIS95 4.2 16.1 1.0 ND1 A:HIS95 4.2 16.4 1.0 CD2 A:HIS118 4.2 15.6 1.0 HH2 A:TRP208 4.2 17.9 1.0 HE2 A:HIS118 4.8 18.2 1.0 HG23 A:THR199 4.9 24.9 1.0 CD A:GLU105 4.9 17.4 1.0 HD1 A:HIS93 4.9 19.5 1.0 HD1 A:HIS95 5.0 19.6 1.0 CA A:HIS118 5.0 15.3 1.0

Zinc binding site 2 out of 2 in the Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Thermostable Variant of Human Carbonic Anhydrase with Tetrazine 2.0 at Site 186 Reacted with Stco in Crystallo within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn306 b:17.1 occ:1.00 O1 B:SO4307 2.0 23.0 0.7 NE2 B:HIS93 2.0 15.8 1.0 ND1 B:HIS118 2.0 15.7 1.0 NE2 B:HIS95 2.0 16.5 1.0 O B:HOH446 2.1 15.8 0.3 O3 B:SO4307 2.8 24.9 0.7 S B:SO4307 2.8 25.6 0.7 CE1 B:HIS118 2.9 15.9 1.0 CD2 B:HIS93 2.9 17.4 1.0 CD2 B:HIS95 3.0 16.9 1.0 CE1 B:HIS93 3.0 16.1 1.0 CE1 B:HIS95 3.0 17.1 1.0 HE1 B:HIS118 3.1 19.0 1.0 CG B:HIS118 3.1 15.7 1.0 HB2 B:HIS118 3.1 18.8 1.0 HD2 B:HIS93 3.1 20.9 1.0 HD2 B:HIS95 3.2 20.2 1.0 HE1 B:HIS95 3.2 20.5 1.0 HE1 B:HIS93 3.2 19.3 1.0 HG1 B:THR198 3.4 20.4 1.0 CB B:HIS118 3.5 15.7 1.0 O B:HOH607 3.6 23.6 0.3 O4 B:SO4307 3.6 27.0 0.7 O B:HOH543 3.7 19.8 0.3 HB3 B:HIS118 3.7 18.8 1.0 OG1 B:THR198 3.9 17.0 1.0 NE2 B:HIS118 4.1 16.0 1.0 OE1 B:GLU105 4.1 18.2 1.0 O2 B:SO4307 4.1 24.5 0.7 ND1 B:HIS93 4.1 16.1 1.0 CG B:HIS93 4.1 16.5 1.0 ND1 B:HIS95 4.1 17.5 1.0 CG B:HIS95 4.1 17.5 1.0 CD2 B:HIS118 4.2 15.9 1.0 O B:HOH648 4.2 38.3 1.0 HH2 B:TRP208 4.3 19.4 1.0 HE2 B:HIS118 4.8 19.2 1.0 HG23 B:THR199 4.9 25.4 1.0 HD1 B:HIS93 4.9 19.3 1.0 HD1 B:HIS95 4.9 21.0 1.0 CD B:GLU105 4.9 18.5 1.0 CA B:HIS118 5.0 16.1 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