Zinc in PDB 6nj4: Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233

Enzymatic activity of Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233

All present enzymatic activity of Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233:
4.2.1.1;

Protein crystallography data

The structure of Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233, PDB code: 6nj4 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) 37.66 / 1.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 44.079, 72.460, 152.108, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 17.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233 (pdb code 6nj4). 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 Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233, PDB code: 6nj4:

Zinc binding site 1 out of 1 in 6nj4

Go back to Zinc Binding Sites List in 6nj4
Zinc binding site 1 out of 1 in the Thermostable Variant of Human Carbonic Anhydrase with Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene 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 Disordered Tetrazine 2.0 Reacted with Strained Trans-Cyclooctene at Site 233 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:12.3
occ:0.40
 O A:HOH521 1.6 14.4 0.6
O A:HOH415 2.0 18.1 0.4
NE2 A:HIS93 2.0 13.4 1.0
NE2 A:HIS95 2.1 11.1 1.0
ND1 A:HIS118 2.1 10.1 1.0
CE1 A:HIS118 2.9 9.8 1.0
CD2 A:HIS93 3.0 13.8 1.0
CE1 A:HIS93 3.0 12.6 1.0
HE1 A:HIS118 3.0 11.8 1.0
CD2 A:HIS95 3.0 10.6 1.0
CE1 A:HIS95 3.1 11.6 1.0
HD2 A:HIS93 3.2 16.5 1.0
HD2 A:HIS95 3.2 12.8 1.0
CG A:HIS118 3.2 9.3 1.0
HE1 A:HIS93 3.2 15.2 1.0
HB2 A:HIS118 3.3 11.0 1.0
HE1 A:HIS95 3.3 14.0 1.0
HG1 A:THR198 3.4 12.3 1.0
CB A:HIS118 3.7 9.2 1.0
OG1 A:THR198 3.7 10.3 1.0
O A:HOH564 3.7 25.8 0.6
HB3 A:HIS118 3.8 11.0 1.0
OE1 A:GLU105 3.9 10.6 1.0
O A:HOH617 3.9 26.5 1.0
NE2 A:HIS118 4.1 10.0 1.0
ND1 A:HIS93 4.1 13.1 1.0
CG A:HIS93 4.1 12.3 1.0
ND1 A:HIS95 4.2 10.8 1.0
CG A:HIS95 4.2 10.6 1.0
O A:HOH675 4.2 27.0 1.0
CD2 A:HIS118 4.2 9.6 1.0
HH2 A:TRP208 4.3 11.4 1.0
CD A:GLU105 4.8 11.4 1.0
HE2 A:HIS118 4.8 12.1 1.0
HD1 A:HIS93 4.9 15.7 1.0
H A:THR198 5.0 11.0 1.0
HD1 A:HIS95 5.0 13.0 1.0
HG23 A:THR199 5.0 17.3 1.0

Reference:

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
Page generated: Wed Dec 16 12:23:52 2020

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