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Magnesium in PDB 4lnl: Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr

Enzymatic activity of Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr

All present enzymatic activity of Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr:
4.1.2.5;

Protein crystallography data

The structure of Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr, PDB code: 4lnl was solved by M.K.Safo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.05 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 76.400, 100.890, 176.000, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 24.3

Other elements in 4lnl:

The structure of Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr (pdb code 4lnl). 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 Complex with Allo- Thr, PDB code: 4lnl:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4lnl

Go back to Magnesium Binding Sites List in 4lnl
Magnesium binding site 1 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr


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 Complex with Allo- Thr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:8.6
occ:1.00
O A:SER196 2.5 11.4 1.0
O A:THR201 2.6 12.7 1.0
OG1 A:THR10 2.7 22.3 1.0
O A:THR10 2.8 18.9 1.0
O A:THR8 2.9 18.6 1.0
C A:SER196 3.5 16.2 1.0
C A:THR10 3.6 21.1 1.0
C A:THR8 3.7 15.7 1.0
N A:THR10 3.7 14.9 1.0
C A:THR201 3.8 14.3 1.0
CB A:THR10 3.8 19.5 1.0
O A:HOH616 3.9 28.8 1.0
CA A:THR10 3.9 16.5 1.0
CA A:SER196 4.0 14.8 1.0
CB A:SER196 4.2 15.8 1.0
CA A:THR8 4.3 14.9 1.0
CA A:PRO202 4.3 11.6 1.0
C A:VAL9 4.4 17.1 1.0
O A:ASP7 4.4 13.2 1.0
N A:THR201 4.4 15.7 1.0
N A:PRO202 4.5 9.3 1.0
O A:LYS197 4.5 19.7 1.0
N A:LYS197 4.5 20.7 1.0
C A:GLY200 4.6 17.7 1.0
N A:VAL9 4.6 17.6 1.0
O A:PRO202 4.6 16.0 1.0
C A:PRO202 4.6 15.0 1.0
CA A:THR201 4.8 16.4 1.0
CA A:LYS197 4.8 17.2 1.0
N A:ARG11 4.8 18.8 1.0
CA A:GLY200 4.8 15.8 1.0
CA A:VAL9 4.9 13.8 1.0
O A:GLY200 4.9 19.0 1.0
CG2 A:THR10 4.9 18.7 1.0

Magnesium binding site 2 out of 3 in 4lnl

Go back to Magnesium Binding Sites List in 4lnl
Magnesium binding site 2 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr


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 Complex with Allo- Thr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:8.9
occ:1.00
O B:THR10 2.6 18.7 1.0
O B:THR201 2.6 17.9 1.0
O B:SER196 2.7 22.2 1.0
O B:THR8 2.8 19.3 1.0
OG1 B:THR10 2.8 17.4 1.0
N B:THR10 3.6 19.1 1.0
C B:THR10 3.6 19.4 1.0
C B:SER196 3.6 20.5 1.0
C B:THR8 3.7 19.4 1.0
C B:THR201 3.8 16.1 1.0
CA B:THR10 3.9 19.7 1.0
CB B:THR10 3.9 20.8 1.0
O B:HOH542 3.9 28.7 1.0
CA B:SER196 4.1 17.7 1.0
CB B:SER196 4.2 18.0 1.0
C B:VAL9 4.3 18.3 1.0
CA B:PRO202 4.4 16.6 1.0
CA B:THR8 4.4 23.4 1.0
O B:ASP7 4.5 13.8 1.0
O B:PRO202 4.5 23.3 1.0
N B:VAL9 4.5 19.3 1.0
N B:PRO202 4.5 17.2 1.0
C B:GLY200 4.6 15.4 1.0
N B:LYS197 4.6 20.4 1.0
N B:THR201 4.6 15.0 1.0
O B:GLY200 4.6 19.2 1.0
O B:LYS197 4.7 21.3 1.0
C B:PRO202 4.7 15.6 1.0
CA B:VAL9 4.7 17.4 1.0
N B:ARG11 4.8 20.8 1.0
CA B:THR201 4.9 15.9 1.0
CA B:LYS197 4.9 18.8 1.0
CG2 B:THR10 5.0 21.0 1.0
CA B:GLY200 5.0 12.2 1.0

Magnesium binding site 3 out of 3 in 4lnl

Go back to Magnesium Binding Sites List in 4lnl
Magnesium binding site 3 out of 3 in the Structure of Escherichia Coli Threonine Aldolase in Complex with Allo- Thr


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 Complex with Allo- Thr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:27.2
occ:1.00
OG B:SER97 2.7 14.9 1.0
O A:HOH707 2.7 26.7 1.0
OG A:SER97 2.8 15.2 1.0
O A:ALA93 2.9 17.4 1.0
O A:VAL94 3.0 12.3 1.0
O B:ALA93 3.3 22.6 1.0
CA B:SER97 3.4 13.0 1.0
CB B:SER97 3.5 11.4 1.0
CA A:SER97 3.5 13.8 1.0
N A:SER97 3.5 15.9 1.0
O B:VAL94 3.6 13.7 1.0
CB A:SER97 3.7 15.0 1.0
N B:SER97 3.7 12.5 1.0
C A:VAL94 3.7 12.9 1.0
C A:ALA93 4.1 13.5 1.0
C B:VAL94 4.3 15.6 1.0
CA A:VAL94 4.3 14.6 1.0
C B:ALA93 4.5 17.3 1.0
C A:LEU95 4.5 10.2 1.0
O A:HOH557 4.5 15.5 1.0
N A:LEU95 4.5 16.0 1.0
O A:LEU95 4.6 12.3 1.0
C A:GLY96 4.6 10.1 1.0
O B:HOH687 4.7 17.2 1.0
N A:GLY96 4.7 13.2 1.0
N A:VAL94 4.7 13.1 1.0
CA A:LEU95 4.8 14.1 1.0
CA B:VAL94 4.8 17.0 1.0
C B:SER97 4.8 15.0 1.0
C B:GLY96 4.9 11.1 1.0
C A:SER97 4.9 11.9 1.0

Reference:

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
Page generated: Mon Dec 14 19:10:01 2020

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