Magnesium in PDB 9hgq: Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic

All present enzymatic activity of Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic:
4.1.3.30;

The structure of Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic, PDB code: 9hgq was solved by W.Stuart, M.Isupov, N.J.Harmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.49 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	73.31, 73.31, 184.141, 90, 90, 120
R / Rfree (%)	18.9 / 24.3

The structure of Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic also contains other interesting chemical elements:

Chlorine

(Cl)

8 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic (pdb code 9hgq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic, PDB code: 9hgq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg309 b:61.8 occ:1.00 O A:HOH401 2.1 54.3 1.0 O A:HOH478 2.1 48.2 1.0 O2 A:MIC301 2.1 48.8 1.0 OD2 A:ASP81 2.1 38.6 1.0 O A:HOH417 2.1 51.7 1.0 C1 A:MIC301 3.0 82.0 1.0 O7 A:MIC301 3.0 91.8 1.0 CG A:ASP81 3.2 34.5 1.0 C2 A:MIC301 3.6 76.5 1.0 OD1 A:ASP81 3.7 38.6 1.0 N A:GLY44 3.8 29.4 1.0 OD1 A:ASP83 3.8 90.0 1.0 CA A:GLY43 3.9 32.1 1.0 N A:GLY43 4.0 31.4 1.0 O1 A:MIC301 4.0 70.1 1.0 OD2 A:ASP54 4.0 40.0 1.0 NH2 A:ARG152 4.2 44.9 1.0 C A:GLY43 4.2 29.2 1.0 CB A:ASP81 4.5 29.1 1.0 OE1 A:GLU110 4.6 63.5 1.0 CG A:ASP83 4.6 65.8 1.0 C3 A:MIC301 4.7 87.9 1.0 OD1 A:ASP54 4.7 38.2 1.0 O5 A:MIC301 4.7 74.5 1.0 CA A:GLY44 4.7 32.5 1.0 CM2 A:MIC301 4.7 63.0 1.0 OD2 A:ASP83 4.7 64.0 1.0 CG A:ASP54 4.8 40.3 1.0 OH A:TYR40 4.9 31.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Coxiella Burnetii 2-Methylisocitrate Lyase Bound to Substrate 2-Mic within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg310 b:51.3 occ:1.00 OD2 B:ASP81 2.1 54.6 1.0 O B:HOH484 2.1 46.0 1.0 O B:HOH459 2.1 39.8 1.0 O2 B:MIC301 2.1 60.8 1.0 O B:HOH431 2.2 49.7 1.0 O7 B:MIC301 2.7 45.7 1.0 C1 B:MIC301 3.2 63.4 1.0 CG B:ASP81 3.2 48.6 1.0 C2 B:MIC301 3.5 50.4 1.0 N B:GLY44 3.7 34.8 1.0 OD1 B:ASP81 3.7 44.0 1.0 CA B:GLY43 3.9 37.5 1.0 OD1 B:ASP83 3.9 93.3 1.0 N B:GLY43 3.9 34.9 1.0 OD2 B:ASP54 4.0 39.5 1.0 NZ B:LYS116 4.0 92.3 1.0 C B:GLY43 4.2 37.4 1.0 C3 B:MIC301 4.3 48.2 1.0 O1 B:MIC301 4.3 48.6 1.0 OD1 B:ASP54 4.4 41.5 1.0 O6 B:MIC301 4.4 52.9 1.0 CB B:ASP81 4.5 34.6 1.0 NH2 B:ARG152 4.5 48.6 1.0 CG B:ASP54 4.6 38.1 1.0 CA B:GLY44 4.6 36.8 1.0 CG B:ASP83 4.7 66.1 1.0 OH B:TYR40 4.8 41.9 1.0 CM2 B:MIC301 4.8 43.0 1.0 C6 B:MIC301 4.8 51.6 1.0 OD2 B:ASP83 4.9 63.1 1.0 OE1 B:GLU110 4.9 47.5 1.0 CE1 B:HIS108 4.9 34.8 1.0

W.S.Stuart, C.H.Jenkins, P.M.Ireland, M.N.Isupov, I.H.Norville, N.J.Harmer. Structure and Catalytic Mechanism of Methylisocitrate Lyase, A Potential Drug Target Against Coxiella Burnetii. J.Biol.Chem. V. 301 08517 2025.
ISSN: ESSN 1083-351X
PubMed: 40250561
DOI: 10.1016/J.JBC.2025.108517