Magnesium in PDB 6x9c: Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site

All present enzymatic activity of Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site:
1.2.1.88; 1.5.5.2;

The structure of Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site, PDB code: 6x9c was solved by J.J.Tanner, A.C.Campbell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.46 / 1.44
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	101.079, 102.253, 127.124, 90, 106.48, 90
R / Rfree (%)	18 / 20.5

The binding sites of Magnesium atom in the Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site (pdb code 6x9c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site, PDB code: 6x9c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1308 b:36.7 occ:1.00 O2A A:NAI1301 2.3 29.6 0.9 O1N A:NAI1301 2.4 27.1 0.9 PN A:NAI1301 3.3 29.6 0.9 PA A:NAI1301 3.5 28.3 0.9 O5B A:NAI1301 3.9 28.9 0.9 O3 A:NAI1301 3.9 26.8 0.9 O2N A:NAI1301 4.0 27.8 0.9 C8A A:NAI1301 4.2 21.8 0.9 OE2 A:GLU733 4.4 40.5 1.0 O A:HOH1618 4.6 40.3 1.0 O A:HOH1787 4.7 27.5 1.0 N7A A:NAI1301 4.8 23.8 0.9 O5D A:NAI1301 4.8 30.6 0.9 O1A A:NAI1301 4.9 29.1 0.9 C5D A:NAI1301 5.0 27.3 0.9

Magnesium binding site 2 out of 2 in the Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Proline Utilization A with L-Proline Bound in the L- Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1306 b:23.8 occ:1.00 O2A B:NAI1301 1.9 21.4 0.6 O1N B:NAI1301 2.0 15.3 0.6 O B:HOH2066 2.1 30.5 1.0 O B:HOH1586 2.5 42.2 1.0 O2A B:NAI1301 3.1 7.7 0.4 PA B:NAI1301 3.2 16.4 0.6 PN B:NAI1301 3.2 17.0 0.6 O3 B:NAI1301 3.6 19.6 0.6 O5B B:NAI1301 4.0 20.9 0.6 C8A B:NAI1301 4.2 16.6 0.4 O B:HOH1651 4.2 58.5 1.0 PA B:NAI1301 4.2 15.0 0.4 C8A B:NAI1301 4.3 17.8 0.6 O2N B:NAI1301 4.4 22.9 0.6 O B:HOH1924 4.4 25.9 1.0 O5B B:NAI1301 4.4 17.8 0.4 C5D B:NAI1301 4.4 22.6 0.6 O5D B:NAI1301 4.4 23.1 0.6 O1A B:NAI1301 4.5 12.1 0.6 CG2 B:VAL786 4.6 21.1 1.0 N7A B:NAI1301 4.6 17.7 0.4 N7A B:NAI1301 4.8 18.2 0.6 O1A B:NAI1301 4.8 16.6 0.4

A.C.Campbell, A.N.Bogner, Y.Mao, D.F.Becker, J.J.Tanner. Structural Analysis of Prolines and Hydroxyprolines Binding to the L-Glutamate-Gamma-Semialdehyde Dehydrogenase Active Site of Bifunctional Proline Utilization A. Arch.Biochem.Biophys. V. 698 08727 2020.
ISSN: ESSN 1096-0384
PubMed: 33333077
DOI: 10.1016/J.ABB.2020.108727