Magnesium in PDB 4b2d: Human PKM2 with L-Serine and Fbp Bound.

All present enzymatic activity of Human PKM2 with L-Serine and Fbp Bound.:
2.7.1.40;

The structure of Human PKM2 with L-Serine and Fbp Bound., PDB code: 4b2d was solved by B.Chaneton, P.Hillmann, L.Zheng, A.C.L.Martin, O.D.K.Maddocks, A.Chokkathukalam, J.E.Coyle, A.Jankevics, F.P.Holding, K.H.Vousden, C.Frezza, M.O'reilly, E.Gottlieb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.85 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.611, 151.098, 91.791, 90.00, 102.01, 90.00
R / Rfree (%)	17.4 / 22.6

The binding sites of Magnesium atom in the Human PKM2 with L-Serine and Fbp Bound. (pdb code 4b2d). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human PKM2 with L-Serine and Fbp Bound., PDB code: 4b2d:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human PKM2 with L-Serine and Fbp Bound.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human PKM2 with L-Serine and Fbp Bound. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg700 b:53.2 occ:1.00 OD2 A:ASP296 2.0 47.2 1.0 OE1 A:GLU272 2.0 47.5 1.0 O A:HOH2237 2.7 33.6 1.0 CD A:GLU272 3.1 43.5 1.0 CG A:ASP296 3.2 46.1 1.0 OE2 A:GLU272 3.5 48.7 1.0 CB A:ASP296 3.8 37.2 1.0 NZ A:LYS270 4.0 32.5 1.0 CZ A:PHE244 4.1 42.0 1.0 O A:HOH2077 4.1 35.7 1.0 OD1 A:ASP296 4.2 50.0 1.0 O A:HOH2144 4.3 37.1 1.0 CG A:GLU272 4.4 51.1 1.0 N A:ASP296 4.5 37.5 1.0 CE1 A:PHE244 4.5 45.0 1.0 O A:HOH2083 4.5 40.3 1.0 CE A:LYS270 4.6 25.8 1.0 CE2 A:PHE244 4.6 42.5 1.0 CB A:GLU272 4.7 44.0 1.0 CA A:ASP296 4.7 35.8 1.0 CB A:ALA293 4.8 38.3 1.0

Magnesium binding site 2 out of 2 in the Human PKM2 with L-Serine and Fbp Bound.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human PKM2 with L-Serine and Fbp Bound. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg700 b:52.0 occ:1.00 OD2 C:ASP296 2.2 58.6 1.0 OE1 C:GLU272 2.3 52.4 1.0 O C:HOH2190 2.7 38.9 1.0 CD C:GLU272 3.1 59.4 1.0 OE2 C:GLU272 3.3 45.3 1.0 CG C:ASP296 3.4 49.9 1.0 NZ C:LYS270 3.9 35.6 1.0 O C:HOH2060 4.0 52.0 1.0 CZ C:PHE244 4.0 48.0 1.0 CB C:ASP296 4.0 38.4 1.0 O C:HOH2069 4.0 39.8 1.0 OD1 C:ASP296 4.4 44.0 1.0 CE1 C:PHE244 4.4 44.1 1.0 CE2 C:PHE244 4.5 50.0 1.0 CG C:GLU272 4.5 44.8 1.0 CE C:LYS270 4.6 31.3 1.0 N C:ASP296 4.7 38.7 1.0 O C:HOH2207 4.7 43.3 1.0 CB C:GLU272 4.9 42.8 1.0

B.Chaneton, P.Hillmann, L.Zheng, A.C.L.Martin, O.D.K.Maddocks, A.Chokkathukalam, J.E.Coyle, A.Jankevics, F.P.Holding, K.H.Vousden, C.Frezza, M.O'reilly, E.Gottlieb. Serine Is A Natural Ligand and Allosteric Activator of Pyruvate Kinase M2. Nature V. 491 458 2012.
ISSN: ESSN 1476-4687
PubMed: 23064226
DOI: 10.1038/NATURE11540