Magnesium in PDB 6so1: Fragment N13569A in Complex with Map Kinase P38-Alpha

All present enzymatic activity of Fragment N13569A in Complex with Map Kinase P38-Alpha:
2.7.11.24;

The structure of Fragment N13569A in Complex with Map Kinase P38-Alpha, PDB code: 6so1 was solved by C.E.Nichols, G.F.De Nicola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.18 / 1.66
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.683, 85.883, 126.807, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 20.4

The structure of Fragment N13569A in Complex with Map Kinase P38-Alpha also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

The binding sites of Magnesium atom in the Fragment N13569A in Complex with Map Kinase P38-Alpha (pdb code 6so1). 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 Fragment N13569A in Complex with Map Kinase P38-Alpha, PDB code: 6so1:

Magnesium binding site 1 out of 1 in the Fragment N13569A in Complex with Map Kinase P38-Alpha


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fragment N13569A in Complex with Map Kinase P38-Alpha within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:29.1 occ:0.57 O A:HOH614 2.0 33.6 1.0 O A:HOH631 2.1 32.5 1.0 OD1 A:ASN155 2.1 27.0 1.0 OD2 A:ASP168 2.2 36.2 1.0 O A:HOH666 2.2 37.2 1.0 O A:HOH503 2.3 37.6 1.0 CG A:ASP168 3.2 35.4 1.0 CG A:ASN155 3.2 28.6 1.0 CB A:ASP168 3.6 30.7 1.0 ND2 A:ASN155 3.8 26.9 1.0 O A:SER154 4.1 24.9 1.0 O4 A:SO4411 4.2 47.0 0.6 O1 A:SO4411 4.2 38.8 0.6 OD1 A:ASP168 4.3 34.3 1.0 CD1 A:LEU167 4.5 35.4 1.0 CB A:ASN155 4.5 23.3 1.0 O2 A:SO4411 4.5 39.8 0.6 OG A:SER154 4.5 25.3 1.0 S A:SO4411 4.5 51.7 0.6 CA A:ASN155 4.6 22.1 1.0 C A:SER154 4.6 24.7 1.0 N A:ASN155 4.8 21.2 1.0 CE A:LYS152 5.0 28.7 1.0

G.F.De Nicola, C.E.Nichols. Targeting the P38 / TAB1 Interface By Single Fragment in-Crystal Screening and Structure-Based Drug Design. To Be Published.