Zinc in PDB 5zzu: Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn

The structure of Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn, PDB code: 5zzu was solved by Y.Q.Zhao, W.Cheng, Y.J.Gu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.83 / 2.10
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	85.060, 85.060, 121.340, 90.00, 90.00, 120.00
R / Rfree (%)	16.5 / 19.7

The binding sites of Zinc atom in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn (pdb code 5zzu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn, PDB code: 5zzu:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn


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 the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:64.9 occ:1.00 O A:ALA299 2.3 20.5 1.0 O A:GLN294 2.4 22.9 1.0 O A:ALA518 2.4 25.2 1.0 O A:THR297 2.4 22.2 1.0 O A:HOH770 2.5 16.8 1.0 O A:HOH749 2.6 18.5 1.0 C A:THR297 3.4 23.3 1.0 C A:PHE298 3.4 21.8 1.0 C A:ALA299 3.4 25.3 1.0 C A:GLN294 3.5 24.4 1.0 N A:ALA299 3.6 23.7 1.0 C A:ALA518 3.6 22.5 1.0 CA A:PHE298 3.7 20.8 1.0 O A:PHE298 3.7 20.6 1.0 N A:PHE298 4.0 22.4 1.0 CA A:ALA299 4.1 24.6 1.0 CA A:GLN294 4.1 22.1 1.0 CA A:GLU519 4.4 22.8 1.0 N A:THR297 4.4 20.8 1.0 N A:GLU519 4.4 22.0 1.0 N A:ALA295 4.5 22.3 1.0 N A:ASN300 4.5 20.7 1.0 CG2 A:ILE521 4.5 21.5 1.0 CA A:THR297 4.5 22.9 1.0 CA A:ALA518 4.5 20.6 1.0 CB A:GLN294 4.6 22.9 1.0 O A:ALA295 4.6 24.8 1.0 OG1 A:THR297 4.6 21.4 1.0 CA A:ALA295 4.6 22.9 1.0 OE1 A:GLU519 4.7 24.8 1.0 C A:ALA295 4.7 20.7 1.0 CB A:ASN300 4.8 21.9 1.0 CA A:ASN300 4.8 24.6 1.0 C A:GLU519 4.9 21.3 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn


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 the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:57.4 occ:1.00 O B:GLN294 2.3 19.3 1.0 O B:ALA518 2.4 23.8 1.0 O B:THR297 2.4 18.6 1.0 O B:HOH779 2.4 18.9 1.0 O B:ALA299 2.4 26.6 1.0 O B:HOH760 2.5 17.9 1.0 C B:GLN294 3.4 19.8 1.0 C B:THR297 3.4 18.9 1.0 C B:PHE298 3.5 20.6 1.0 C B:ALA299 3.5 26.1 1.0 C B:ALA518 3.6 21.0 1.0 N B:ALA299 3.7 22.9 1.0 CA B:PHE298 3.8 19.6 1.0 O B:PHE298 3.9 22.6 1.0 N B:PHE298 4.0 23.6 1.0 CA B:GLN294 4.1 20.3 1.0 CA B:ALA299 4.2 26.8 1.0 N B:ALA295 4.3 20.3 1.0 N B:THR297 4.4 19.2 1.0 CG2 B:ILE521 4.4 19.4 1.0 CA B:GLU519 4.4 19.3 1.0 N B:GLU519 4.4 19.5 1.0 CA B:ALA518 4.5 21.8 1.0 CA B:THR297 4.5 22.3 1.0 CA B:ALA295 4.5 22.0 1.0 CB B:GLN294 4.5 16.3 1.0 O B:ALA295 4.5 20.7 1.0 C B:ALA295 4.5 20.3 1.0 N B:ASN300 4.6 23.5 1.0 OG1 B:THR297 4.6 21.5 1.0 OE1 B:GLU519 4.7 27.1 1.0 CB B:ASN300 4.9 25.9 1.0 C B:GLU519 4.9 21.4 1.0 CA B:ASN300 4.9 25.1 1.0 N B:LEU520 4.9 20.9 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn601 b:55.5 occ:1.00 O C:GLN294 2.4 19.9 1.0 O C:THR297 2.4 22.5 1.0 O C:ALA518 2.4 24.6 1.0 O C:ALA299 2.4 19.8 1.0 O C:HOH806 2.5 21.7 1.0 O C:HOH720 2.8 18.6 1.0 C C:THR297 3.4 23.2 1.0 C C:GLN294 3.4 19.3 1.0 C C:PHE298 3.5 19.2 1.0 C C:ALA299 3.5 21.4 1.0 C C:ALA518 3.6 26.7 1.0 N C:ALA299 3.6 20.4 1.0 CA C:PHE298 3.7 19.9 1.0 O C:PHE298 3.9 23.4 1.0 N C:PHE298 4.0 20.0 1.0 CA C:GLN294 4.1 20.1 1.0 CA C:ALA299 4.2 23.0 1.0 N C:ALA295 4.4 20.7 1.0 N C:THR297 4.4 18.6 1.0 CG2 C:ILE521 4.4 21.2 1.0 CA C:GLU519 4.5 25.2 1.0 N C:GLU519 4.5 21.6 1.0 CA C:ALA518 4.5 24.5 1.0 CB C:GLN294 4.5 20.1 1.0 CA C:THR297 4.5 23.4 1.0 N C:ASN300 4.5 22.1 1.0 CA C:ALA295 4.6 22.5 1.0 O C:ALA295 4.6 21.5 1.0 C C:ALA295 4.6 20.7 1.0 OG1 C:THR297 4.7 21.6 1.0 CB C:ASN300 4.8 21.8 1.0 OE1 C:GLU519 4.8 26.1 1.0 CA C:ASN300 4.8 22.5 1.0 C C:GLU519 4.9 22.8 1.0

Y.Q.Zhao, Y.J.Lai, D.Zhou, C.Dou, Y.J.Gu, C.L.Nie, Y.Q.Wei, W.Cheng. Structural and Mechanistic Insights Into Polymyxin Resistance Mediated By Eptc Originating From Escherichia Coli To Be Published.