Zinc in PDB 8sjg: Zn-Bound Structure of Computationally Designed Homotrimer TET4

The structure of Zn-Bound Structure of Computationally Designed Homotrimer TET4, PDB code: 8sjg was solved by A.M.Hoffnagle, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.83 / 2.39
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	67.663, 67.663, 109.635, 90, 90, 120
R / Rfree (%)	24 / 28.6

The binding sites of Zinc atom in the Zn-Bound Structure of Computationally Designed Homotrimer TET4 (pdb code 8sjg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zn-Bound Structure of Computationally Designed Homotrimer TET4, PDB code: 8sjg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Zn-Bound Structure of Computationally Designed Homotrimer TET4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Bound Structure of Computationally Designed Homotrimer TET4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:46.9 occ:0.33 NE2 A:HIS38 2.0 55.6 1.0 O A:HOH311 2.0 37.9 0.3 CE1 A:HIS38 2.9 48.8 1.0 CD2 A:HIS38 3.1 39.0 1.0 ND1 A:HIS38 4.1 42.1 1.0 CG A:HIS38 4.2 54.2 1.0 CD1 A:LEU42 4.4 94.6 1.0

Zinc binding site 2 out of 2 in the Zn-Bound Structure of Computationally Designed Homotrimer TET4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zn-Bound Structure of Computationally Designed Homotrimer TET4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:107.9 occ:0.33 O B:HOH304 2.0 91.4 0.3 NE2 B:HIS38 2.1 149.0 1.0 CE1 B:HIS38 2.8 139.7 1.0 CD2 B:HIS38 3.3 137.4 1.0 ND1 B:HIS38 4.0 143.6 1.0 CG B:HIS38 4.3 141.6 1.0

A.M.Hoffnagle, F.A.Tezcan. Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries. J.Am.Chem.Soc. 2023.
ISSN: ESSN 1520-5126
PubMed: 37352018
DOI: 10.1021/JACS.3C04047