Zinc in PDB 8c2o: Structure of E. Coli Amia

All present enzymatic activity of Structure of E. Coli Amia:
3.5.1.28;

The structure of Structure of E. Coli Amia, PDB code: 8c2o was solved by T.C.Baverstock, A.Crow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.59 / 2.35
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.515, 73.899, 115.563, 90, 90, 90
R / Rfree (%)	17.7 / 23.6

The binding sites of Zinc atom in the Structure of E. Coli Amia (pdb code 8c2o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of E. Coli Amia, PDB code: 8c2o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of E. Coli Amia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of E. Coli Amia within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:41.8 occ:1.00 OE2 A:GLU80 2.1 29.4 1.0 NE2 A:HIS65 2.2 35.8 1.0 OD2 A:ASP135 2.2 45.2 1.0 OE1 A:GLU167 2.3 44.5 1.0 ND1 A:HIS133 2.3 34.6 1.0 OE2 A:GLU167 2.4 47.2 1.0 CD A:GLU167 2.6 50.4 1.0 CD A:GLU80 2.9 31.4 1.0 OE1 A:GLU80 3.1 35.1 1.0 CG A:ASP135 3.2 44.6 1.0 CE1 A:HIS65 3.2 38.2 1.0 CG A:HIS133 3.2 31.9 1.0 CD2 A:HIS65 3.2 36.9 1.0 CE1 A:HIS133 3.3 38.7 1.0 CB A:ASP135 3.4 37.7 1.0 CB A:HIS133 3.4 32.9 1.0 CG A:GLU167 4.1 42.1 1.0 O A:HOH409 4.2 50.5 1.0 CA A:ASP135 4.3 37.6 1.0 ND1 A:HIS65 4.3 37.9 1.0 CD2 A:HIS133 4.3 32.6 1.0 CG A:GLU80 4.3 28.6 1.0 CG A:HIS65 4.3 37.3 1.0 CA A:HIS133 4.3 34.9 1.0 OD1 A:ASP135 4.4 38.6 1.0 NE2 A:HIS133 4.4 33.1 1.0 N A:ALA134 4.5 41.5 1.0 N A:ASP135 4.5 34.6 1.0 O A:HOH429 4.6 31.3 1.0 OE2 A:GLU242 4.6 41.3 1.0 OE1 A:GLU242 4.8 37.7 1.0 C A:HIS133 5.0 38.7 1.0 C A:ALA134 5.0 35.0 1.0

Zinc binding site 2 out of 2 in the Structure of E. Coli Amia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of E. Coli Amia within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:42.7 occ:1.00 OE2 B:GLU80 2.1 33.7 1.0 NE2 B:HIS65 2.2 35.5 1.0 OE2 B:GLU167 2.3 43.5 1.0 OE1 B:GLU167 2.3 41.1 1.0 ND1 B:HIS133 2.3 35.8 1.0 OD2 B:ASP135 2.4 50.5 1.0 CD B:GLU167 2.6 40.9 1.0 CD B:GLU80 3.0 43.1 1.0 CE1 B:HIS65 3.2 39.8 1.0 CG B:HIS133 3.2 30.0 1.0 CD2 B:HIS65 3.2 37.4 1.0 CG B:ASP135 3.2 51.7 1.0 OE1 B:GLU80 3.2 35.8 1.0 CE1 B:HIS133 3.3 36.2 1.0 CB B:HIS133 3.3 30.1 1.0 CB B:ASP135 3.4 47.8 1.0 CG B:GLU167 4.1 38.9 1.0 ND1 B:HIS65 4.3 28.3 1.0 CA B:ASP135 4.3 45.8 1.0 CG B:HIS65 4.3 33.3 1.0 CA B:HIS133 4.3 36.3 1.0 CD2 B:HIS133 4.3 40.1 1.0 CG B:GLU80 4.3 40.5 1.0 NE2 B:HIS133 4.4 38.2 1.0 OD1 B:ASP135 4.4 42.1 1.0 O B:HOH416 4.5 39.3 1.0 N B:ALA134 4.5 41.3 1.0 N B:ASP135 4.5 42.4 1.0 OE2 B:GLU242 4.7 43.3 1.0 OE1 B:GLU242 4.8 33.6 1.0 C B:HIS133 5.0 39.4 1.0

J.Cook, T.C.Baverstock, M.B.L.Mcandrew, D.I.Roper, P.J.Stansfeld, A.Crow. Activator-Induced Conformational Changes Regulate Division-Associated Peptidoglycan Amidases. Proc.Natl.Acad.Sci.Usa V. 120 80120 2023.
ISSN: ESSN 1091-6490
PubMed: 37276423
DOI: 10.1073/PNAS.2302580120