Zinc in PDB 7rsf: Acetylornithine Deacetylase From Escherichia Coli

All present enzymatic activity of Acetylornithine Deacetylase From Escherichia Coli:
3.5.1.16;

The structure of Acetylornithine Deacetylase From Escherichia Coli, PDB code: 7rsf was solved by J.Osipiuk, M.Endres, D.P.Becker, A.Joachimiak, Center For Structuralgenomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.15 / 2.13
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	46.7, 70.994, 289.884, 90, 90, 90
R / Rfree (%)	18.8 / 23.4

The structure of Acetylornithine Deacetylase From Escherichia Coli also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Acetylornithine Deacetylase From Escherichia Coli (pdb code 7rsf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Acetylornithine Deacetylase From Escherichia Coli, PDB code: 7rsf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Acetylornithine Deacetylase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acetylornithine Deacetylase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:39.8 occ:1.00 OD1 A:ASP112 1.9 37.1 1.0 O A:HOH655 2.0 36.4 1.0 NE2 A:HIS80 2.1 37.9 1.0 OE1 A:GLU169 2.1 37.2 1.0 CG A:ASP112 2.8 41.3 1.0 CD A:GLU169 2.8 38.4 1.0 OE2 A:GLU169 2.8 36.6 1.0 CE1 A:HIS80 2.9 39.2 1.0 OD2 A:ASP112 3.0 45.0 1.0 CD2 A:HIS80 3.2 38.2 1.0 OE1 A:GLU144 3.8 35.6 1.0 OE2 A:GLU145 3.9 50.0 1.0 O A:HOH641 4.1 47.7 1.0 ND1 A:HIS80 4.1 38.2 1.0 CB A:ASP112 4.2 40.9 1.0 CG A:GLU169 4.2 39.2 1.0 CG A:HIS80 4.3 37.2 1.0 CD A:GLU144 4.3 39.1 1.0 CG A:MET113 4.3 41.0 1.0 SD A:MET113 4.5 40.0 1.0 CD A:PRO170 4.5 47.3 1.0 CB A:MET113 4.5 40.8 1.0 CD A:GLU145 4.6 47.3 1.0 CA A:ASP112 4.6 41.7 1.0 OE2 A:GLU144 4.7 41.3 1.0 C A:ASP112 4.7 42.9 1.0 CB A:GLU169 4.8 38.4 1.0 O A:ASP112 4.9 43.2 1.0 CA A:GLU169 4.9 40.5 1.0

Zinc binding site 2 out of 2 in the Acetylornithine Deacetylase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Acetylornithine Deacetylase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:37.1 occ:1.00 OD1 B:ASP112 1.9 39.6 1.0 NE2 B:HIS80 2.1 34.6 1.0 O B:HOH532 2.1 33.7 1.0 OE1 B:GLU169 2.1 39.9 1.0 OE2 B:GLU169 2.7 39.9 1.0 CD B:GLU169 2.7 36.7 1.0 CG B:ASP112 2.8 39.5 1.0 CE1 B:HIS80 3.0 35.3 1.0 CD2 B:HIS80 3.1 36.0 1.0 OD2 B:ASP112 3.1 45.9 1.0 OE1 B:GLU144 3.6 45.5 1.0 OE2 B:GLU145 3.8 42.0 1.0 O B:HOH563 3.9 52.0 1.0 ND1 B:HIS80 4.1 35.6 1.0 CB B:ASP112 4.2 39.2 1.0 CG B:GLU169 4.2 37.0 1.0 CG B:HIS80 4.2 35.6 1.0 CG B:MET113 4.3 38.5 1.0 CD B:GLU144 4.3 45.6 1.0 SD B:MET113 4.4 37.5 1.0 CD B:PRO170 4.4 38.6 1.0 CB B:MET113 4.5 39.2 1.0 CA B:ASP112 4.6 39.4 1.0 CD B:GLU145 4.6 41.2 1.0 C B:ASP112 4.7 40.9 1.0 OE2 B:GLU144 4.8 50.0 1.0 CB B:GLU169 4.8 38.3 1.0 O B:ASP112 4.9 38.1 1.0 CA B:GLU169 5.0 37.4 1.0

J.Osipiuk, M.Endres, D.P.Becker, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Acetylornithine Deacetylase From Escherichia Coli To Be Published.