Zinc in PDB 8e2r: Crystal Structure of Tadac-1.14

All present enzymatic activity of Crystal Structure of Tadac-1.14:
3.5.4.33;

The structure of Crystal Structure of Tadac-1.14, PDB code: 8e2r was solved by P.R.Feliciano, S.J.Lee, G.Ciaramella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.21 / 2.22
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.74, 89.74, 112, 90, 90, 90
R / Rfree (%)	21.6 / 25.1

The binding sites of Zinc atom in the Crystal Structure of Tadac-1.14 (pdb code 8e2r). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Tadac-1.14, PDB code: 8e2r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Tadac-1.14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Tadac-1.14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:54.2 occ:1.00 ND1 A:HIS57 2.0 50.4 1.0 O A:HOH310 2.1 58.3 1.0 SG A:CYS87 2.2 48.3 1.0 SG A:CYS90 2.3 50.9 1.0 CE1 A:HIS57 2.9 52.3 1.0 CG A:HIS57 3.1 51.3 1.0 CB A:CYS90 3.2 47.4 1.0 CB A:CYS87 3.4 55.5 1.0 CB A:HIS57 3.5 43.2 1.0 N A:CYS87 3.7 53.2 1.0 N A:CYS90 3.9 45.1 1.0 CE A:MET89 3.9 46.4 1.0 NE2 A:HIS57 4.1 52.7 1.0 CA A:CYS87 4.1 50.4 1.0 CD2 A:HIS57 4.2 49.8 1.0 CA A:CYS90 4.2 47.2 1.0 O A:HOH316 4.3 69.3 1.0 OE1 A:GLU59 4.3 55.8 1.0 O A:HOH312 4.4 64.6 1.0 OE2 A:GLU59 4.5 62.1 1.0 CD A:GLU59 4.6 57.9 1.0 C A:CYS87 4.6 45.4 1.0 O A:CYS87 4.8 47.5 1.0 C A:PRO86 4.8 52.2 1.0 CA A:PRO86 5.0 60.1 1.0 CB A:MET89 5.0 47.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Tadac-1.14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Tadac-1.14 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:53.0 occ:1.00 ND1 B:HIS57 2.0 42.6 1.0 O B:HOH306 2.0 52.9 1.0 SG B:CYS90 2.3 54.1 1.0 SG B:CYS87 2.3 56.2 1.0 CE1 B:HIS57 2.9 54.8 1.0 CG B:HIS57 3.0 62.5 1.0 CB B:CYS90 3.2 46.1 1.0 CB B:HIS57 3.4 44.5 1.0 CB B:CYS87 3.5 47.3 1.0 N B:CYS87 3.8 56.4 1.0 O B:HOH312 3.8 66.9 1.0 CE B:MET89 3.9 50.9 1.0 OE2 B:GLU59 3.9 67.6 1.0 N B:CYS90 4.0 50.0 1.0 NE2 B:HIS57 4.1 47.3 1.0 OE1 B:GLU59 4.1 57.0 1.0 CD2 B:HIS57 4.1 51.5 1.0 CA B:CYS87 4.2 47.7 1.0 CA B:CYS90 4.2 52.9 1.0 CD B:GLU59 4.2 60.8 1.0 O B:HOH321 4.3 66.3 1.0 C B:CYS87 4.7 51.9 1.0 O B:CYS87 4.8 49.3 1.0 C B:PRO86 4.9 54.5 1.0 CA B:HIS57 4.9 45.2 1.0 CB B:MET89 5.0 50.3 1.0

D.K.Lam, P.R.Feliciano, A.Arif, T.Bohnuud, T.P.Fernandez, J.M.Gehrke, P.Grayson, K.D.Lee, M.A.Ortega, C.Sawyer, N.Schwaegerle, L.Peraro, L.Young, S.J.Lee, G.Ciaramella, N.M.Gaudelli. Improved Cytosine Base Editors Generated From Tada Variants Nat.Biotechnol. 2023.
ISSN: ISSN 1087-0156