Magnesium in PDB 4adb: Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli

All present enzymatic activity of Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli:
2.6.1.17; 2.6.1.81;

The structure of Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli, PDB code: 4adb was solved by J.Newman, T.S.Peat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	109.05 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	184.708, 118.428, 109.792, 90.00, 96.69, 90.00
R / Rfree (%)	17.085 / 21.885

The structure of Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli also contains other interesting chemical elements:

Sodium

(Na)

4 atoms

The binding sites of Magnesium atom in the Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli (pdb code 4adb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli, PDB code: 4adb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1999 b:27.9 occ:0.50 O A:HOH2111 2.2 26.9 1.0 O A:HOH2222 2.2 31.0 1.0 O A:HOH2220 2.4 24.3 1.0 O A:HOH2223 2.4 33.0 1.0 O A:HOH2110 2.4 24.2 1.0 O A:HOH2221 2.6 39.5 1.0 NZ C:LYS118 3.6 28.0 1.0 NZ A:LYS118 3.8 26.6 1.0 CE A:LYS118 4.1 28.2 1.0 O A:HOH2092 4.2 33.4 1.0 OD2 B:ASP157 4.4 29.3 1.0 OD1 B:ASP157 4.5 33.1 1.0 OD2 D:ASP157 4.5 35.6 1.0 OD2 A:ASP122 4.6 29.4 1.0 CE C:LYS118 4.6 26.4 1.0 OD1 A:ASP122 4.6 21.9 1.0 OD1 D:ASP157 4.8 43.6 1.0 CG B:ASP157 4.9 31.5 1.0 OD2 C:ASP122 4.9 29.9 1.0 OG1 C:THR274 4.9 25.5 1.0 OD1 C:ASP122 5.0 23.0 1.0 CG A:ASP122 5.0 24.7 1.0 OG1 A:THR274 5.0 20.6 1.0

Magnesium binding site 2 out of 2 in the Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural and Functional Study of Succinyl-Ornithine Transaminase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1999 b:38.8 occ:0.50 O A:HOH2137 2.4 26.4 1.0 O A:HOH2138 2.4 23.2 1.0 O B:HOH2073 2.6 23.3 1.0 NZ B:LYS118 3.5 21.3 1.0 O B:HOH2035 4.0 22.4 0.5 O A:HOH2056 4.1 19.4 1.0 CE B:LYS118 4.2 24.7 1.0 OD2 A:ASP157 4.6 29.6 1.0 OD1 A:ASP157 4.7 28.2 1.0 OD1 B:ASP122 4.7 17.8 1.0 OD2 B:ASP122 4.8 21.9 1.0 OG1 B:THR274 4.9 20.2 1.0

J.Newman, S.Seabrook, R.Surjadi, C.C.Williams, D.Lucent, M.Wilding, C.Scott, T.S.Peat. Determination of the Structure of the Catabolic N- Succinylornithine Transaminase (Astc) From Escherichia Coli. Plos One V. 8 58298 2013.
ISSN: ISSN 1932-6203
PubMed: 23484010
DOI: 10.1371/JOURNAL.PONE.0058298