Magnesium in PDB 4lnj: Structure of Escherichia Coli Threonine Aldolase in Unliganded Form

All present enzymatic activity of Structure of Escherichia Coli Threonine Aldolase in Unliganded Form:
4.1.2.5;

The structure of Structure of Escherichia Coli Threonine Aldolase in Unliganded Form, PDB code: 4lnj was solved by M.K.Safo, R.Contestabile, S.G.Remesh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.35 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	76.620, 100.790, 176.080, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 27.9

The binding sites of Magnesium atom in the Structure of Escherichia Coli Threonine Aldolase in Unliganded Form (pdb code 4lnj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of Escherichia Coli Threonine Aldolase in Unliganded Form, PDB code: 4lnj:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Unliganded Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Escherichia Coli Threonine Aldolase in Unliganded Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:20.3 occ:1.00 O A:THR10 2.6 25.4 1.0 O A:SER196 2.6 14.7 1.0 O A:THR201 2.7 24.3 1.0 OG1 A:THR10 2.8 27.0 1.0 O A:THR8 2.9 23.1 1.0 C A:THR10 3.5 29.6 1.0 N A:THR10 3.6 21.1 1.0 C A:SER196 3.7 16.4 1.0 C A:THR8 3.7 27.6 1.0 C A:THR201 3.8 22.0 1.0 CB A:THR10 3.8 29.4 1.0 CA A:THR10 3.8 24.7 1.0 CA A:PRO202 4.2 21.9 1.0 C A:VAL9 4.3 17.6 1.0 CA A:SER196 4.3 18.2 1.0 O A:PRO202 4.3 30.1 1.0 CA A:THR8 4.4 25.8 1.0 N A:PRO202 4.4 21.3 1.0 CB A:SER196 4.5 19.9 1.0 C A:PRO202 4.6 23.5 1.0 N A:THR201 4.6 22.1 1.0 N A:VAL9 4.6 25.7 1.0 O A:ASP7 4.7 19.7 1.0 N A:ARG11 4.7 27.1 1.0 O A:LYS197 4.8 30.5 1.0 CA A:VAL9 4.8 22.1 1.0 N A:LYS197 4.8 25.6 1.0 C A:GLY200 4.8 24.4 1.0 CA A:THR201 4.8 20.0 1.0 O A:VAL9 4.9 24.7 1.0 CA A:LYS197 4.9 28.3 1.0

Magnesium binding site 2 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Unliganded Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Escherichia Coli Threonine Aldolase in Unliganded Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:23.7 occ:1.00 OG A:SER97 2.7 18.0 1.0 O A:HOH523 2.8 21.3 1.0 OG B:SER97 2.8 19.7 1.0 O B:ALA93 3.0 23.5 1.0 O A:ALA93 3.0 18.9 1.0 O A:VAL94 3.2 13.4 1.0 O B:VAL94 3.4 19.1 1.0 CA A:SER97 3.5 20.3 1.0 CA B:SER97 3.5 16.4 1.0 CB A:SER97 3.6 22.2 1.0 CB B:SER97 3.6 12.5 1.0 N A:SER97 3.6 23.3 1.0 N B:SER97 3.7 17.5 1.0 C A:VAL94 3.9 12.3 1.0 C B:VAL94 4.0 14.1 1.0 C B:ALA93 4.2 22.0 1.0 C A:ALA93 4.2 17.1 1.0 CA B:VAL94 4.4 15.5 1.0 O A:HOH608 4.5 27.4 1.0 CA A:VAL94 4.5 12.8 1.0 O A:LEU95 4.6 17.9 1.0 C A:LEU95 4.7 13.4 1.0 C A:GLY96 4.8 21.5 1.0 N A:LEU95 4.8 11.6 1.0 N B:VAL94 4.8 16.8 1.0 O B:HOH619 4.8 35.2 1.0 N A:VAL94 4.8 18.4 1.0 N B:LEU95 4.9 17.6 1.0 C A:SER97 4.9 17.6 1.0 C B:SER97 4.9 17.5 1.0 C B:GLY96 4.9 18.9 1.0 C B:LEU95 5.0 21.0 1.0

Magnesium binding site 3 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Unliganded Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Escherichia Coli Threonine Aldolase in Unliganded Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:21.2 occ:1.00 O B:THR201 2.7 22.9 1.0 O B:THR10 2.7 28.4 1.0 OG1 B:THR10 2.8 24.7 1.0 O B:SER196 2.8 30.4 1.0 O B:THR8 3.3 33.5 1.0 C B:SER196 3.7 22.6 1.0 C B:THR10 3.7 25.9 1.0 N B:THR10 3.8 30.8 1.0 C B:THR201 3.9 25.7 1.0 C B:THR8 3.9 29.2 1.0 CB B:THR10 4.0 29.0 1.0 CA B:SER196 4.0 19.9 1.0 CA B:THR10 4.0 23.8 1.0 CB B:SER196 4.2 23.3 1.0 C B:VAL9 4.3 26.3 1.0 CA B:PRO202 4.5 25.3 1.0 O B:PRO202 4.5 29.0 1.0 CA B:THR8 4.6 29.8 1.0 N B:VAL9 4.6 27.1 1.0 N B:THR201 4.6 25.1 1.0 C B:PRO202 4.6 23.2 1.0 N B:PRO202 4.6 25.3 1.0 C B:GLY200 4.7 27.9 1.0 O B:LYS197 4.7 24.9 1.0 O B:ASP7 4.7 27.5 1.0 CA B:VAL9 4.8 29.8 1.0 N B:LYS197 4.8 28.1 1.0 O B:VAL9 4.8 26.2 1.0 CA B:THR201 4.9 24.4 1.0 N B:ARG11 4.9 25.8 1.0 CG2 B:THR10 5.0 29.6 1.0

M.L.Di Salvo, S.G.Remesh, M.Vivoli, M.S.Ghatge, A.Paiardini, S.D'aguanno, M.K.Safo, R.Contestabile. On the Catalytic Mechanism and Stereospecificity of Escherichia Coli L-Threonine Aldolase. Febs J. V. 281 129 2014.
ISSN: ISSN 1742-464X
PubMed: 24165453
DOI: 10.1111/FEBS.12581