Magnesium in PDB 9dl3: Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid

All present enzymatic activity of Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid:
1.2.1.88; 1.5.5.2;

The structure of Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid, PDB code: 9dl3 was solved by J.J.Tanner, K.R.Meeks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.53 / 1.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	100.961, 102.33, 127.061, 90, 105.96, 90
R / Rfree (%)	17.7 / 21.3

The binding sites of Magnesium atom in the Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid (pdb code 9dl3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid, PDB code: 9dl3:

Magnesium binding site 1 out of 1 in the Structure of Proline Utilization A Complexed with Quinoline-2- Carboxylic Acid


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 Complexed with Quinoline-2- Carboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2020 b:28.7 occ:1.00 O A:HOH2337 2.1 24.6 1.0 O2 A:QNC2003 2.1 27.7 0.9 O A:HOH2269 2.1 29.0 1.0 O A:HOH2998 2.1 33.2 1.0 N1 A:QNC2003 2.3 23.4 0.9 C A:QNC2003 2.9 25.4 0.9 C2 A:QNC2003 3.0 22.5 0.9 C8A A:QNC2003 3.3 25.4 0.9 C8 A:QNC2003 3.5 28.6 0.9 O A:QNC2003 4.2 28.1 0.9 OE1 A:GLU733 4.2 30.4 1.0 O A:HOH2380 4.2 31.8 1.0 N A:GLY763 4.2 22.6 1.0 OE2 A:GLU733 4.3 34.1 1.0 C3 A:QNC2003 4.4 24.9 0.9 CB A:ASP762 4.6 26.2 1.0 C4A A:QNC2003 4.6 25.6 0.9 CD A:GLU733 4.7 33.3 1.0 CA A:GLY763 4.8 22.4 1.0 C7 A:QNC2003 4.9 29.2 0.9

K.R.Meeks, A.N.Bogner, J.C.Nix, J.J.Tanner. Crystallographic Fragment Screening of A Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates For Proline Dehydrogenase and L-Glutamate-Gamma-Semialdehyde Dehydrogenase Molecules V. 29 2024.
ISSN: ESSN 1420-3049
DOI: 10.3390/MOLECULES29225408