Magnesium in PDB 7mbh: Structure of Human Enolase 2 in Complex with Phosphoserine

All present enzymatic activity of Structure of Human Enolase 2 in Complex with Phosphoserine:
4.2.1.11;

The structure of Structure of Human Enolase 2 in Complex with Phosphoserine, PDB code: 7mbh was solved by P.G.Leonard, K.G.Hicks, J.Rutter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.39 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.05, 108.38, 117.929, 90, 90, 90
R / Rfree (%)	18 / 23.5

The binding sites of Magnesium atom in the Structure of Human Enolase 2 in Complex with Phosphoserine (pdb code 7mbh). 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 Human Enolase 2 in Complex with Phosphoserine, PDB code: 7mbh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Enolase 2 in Complex with Phosphoserine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Enolase 2 in Complex with Phosphoserine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:23.8 occ:1.00 O A:HOH730 1.9 29.5 1.0 OD2 A:ASP318 2.1 25.2 1.0 OD2 A:ASP245 2.1 29.6 1.0 OE2 A:GLU293 2.2 26.1 1.0 O A:HOH670 2.2 21.8 1.0 O A:HOH711 2.3 27.6 1.0 CG A:ASP245 3.1 24.0 1.0 CG A:ASP318 3.2 23.2 1.0 CD A:GLU293 3.3 24.8 1.0 OD1 A:ASP245 3.3 24.0 1.0 CB A:ASP318 3.7 19.3 1.0 NZ A:LYS394 3.8 25.8 1.0 OE1 A:GLU293 4.0 24.6 1.0 OD1 A:ASP318 4.2 22.1 1.0 CG A:GLU293 4.2 22.0 1.0 NZ A:LYS343 4.3 22.8 1.0 NE2 A:GLN166 4.4 31.0 1.0 OXT A:ACT503 4.4 42.6 1.0 CB A:ASP245 4.4 22.5 1.0 CD2 A:LEU341 4.5 19.5 1.0 OD2 A:ASP294 4.6 26.0 1.0 OE2 A:GLU167 4.7 44.7 1.0 CE A:LYS394 4.9 22.7 1.0 OE1 A:GLU167 4.9 40.6 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Enolase 2 in Complex with Phosphoserine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Enolase 2 in Complex with Phosphoserine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:30.8 occ:1.00 OE2 B:GLU293 2.1 28.9 1.0 OD2 B:ASP245 2.1 31.9 1.0 O B:HOH665 2.1 34.0 1.0 OD2 B:ASP318 2.2 22.8 1.0 O B:HOH628 2.3 25.8 1.0 O B:HOH700 2.3 30.6 1.0 CG B:ASP245 3.1 31.1 1.0 CD B:GLU293 3.2 30.8 1.0 CG B:ASP318 3.2 24.0 1.0 OD1 B:ASP245 3.5 29.1 1.0 CB B:ASP318 3.8 21.2 1.0 NZ B:LYS394 3.9 30.2 1.0 OE1 B:GLU293 4.0 30.3 1.0 CG B:GLU293 4.1 23.0 1.0 OD1 B:ASP318 4.2 18.9 1.0 OD2 B:ASP294 4.4 32.6 1.0 OE1 B:GLN166 4.4 42.3 1.0 NZ B:LYS343 4.4 23.5 1.0 CB B:ASP245 4.4 29.0 1.0 CD2 B:LEU341 4.5 26.9 1.0 OXT B:SEP501 4.8 51.1 1.0 OE1 B:GLU167 4.8 44.1 1.0 O2P B:SEP501 4.9 39.8 1.0 CE B:LYS394 4.9 26.3 1.0

K.G.Hick, P.G.Leonard, J.Rutter. The Protein-Metabolite Interactome of Central Carbon Metabolism Reveals Novel Regulation of Pyruvate Metabolism To Be Published.