Magnesium in PDB 4nm3: Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide

All present enzymatic activity of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide:
2.7.11.1; 2.7.11.26;

The structure of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide, PDB code: 4nm3 was solved by M.L.-H.Chu, J.L.Stamos, M.D.Enos, N.Shah, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.96 / 2.10
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	81.032, 81.032, 281.085, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24.2

The structure of Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide (pdb code 4nm3). 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 Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide, PDB code: 4nm3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide


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 Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg405 b:51.1 occ:1.00 O A:HOH671 2.0 47.6 1.0 O1A A:ADP409 2.1 48.0 0.8 OD1 A:ASN186 2.1 33.4 1.0 OD2 A:ASP200 2.2 43.7 1.0 O A:HOH584 2.3 51.4 1.0 O1B A:ADP409 2.3 48.3 0.8 CG A:ASN186 3.1 34.2 1.0 PA A:ADP409 3.2 46.3 0.8 CG A:ASP200 3.2 41.5 1.0 O3A A:ADP409 3.3 0.7 0.8 ND2 A:ASN186 3.4 30.9 1.0 PB A:ADP409 3.5 48.3 0.8 CB A:ASP200 3.5 38.5 1.0 O5' A:ADP409 3.5 58.2 0.8 O A:HOH532 4.1 40.4 1.0 O A:HOH668 4.2 76.0 1.0 O3' A:ADP409 4.3 46.6 0.8 OD1 A:ASP200 4.3 43.2 1.0 O3B A:ADP409 4.4 49.6 0.8 CB A:ASN186 4.5 31.7 1.0 O2A A:ADP409 4.5 43.4 0.8 O2B A:ADP409 4.5 52.8 0.8 OD2 A:ASP181 4.5 36.3 1.0 C3' A:ADP409 4.7 49.2 0.8 MG A:MG406 4.8 56.5 1.0 CA A:ASN186 4.8 31.8 1.0 CE A:LYS183 4.8 36.7 1.0 O A:GLN185 4.8 35.0 1.0 O A:HOH669 4.8 63.8 1.0 C5' A:ADP409 4.9 51.6 0.8 O A:HOH533 4.9 41.5 1.0 CA A:ASP200 5.0 37.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide


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 Gsk-3/Axin Complex Bound to Phosphorylated N- Terminal Auto-Inhibitory PS9 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg406 b:56.5 occ:1.00 O3B A:ADP409 2.2 49.6 0.8 OD1 A:ASP200 2.3 43.2 1.0 O A:HOH532 2.5 40.4 1.0 O A:HOH533 2.8 41.5 1.0 OD2 A:ASP200 2.9 43.7 1.0 CG A:ASP200 2.9 41.5 1.0 PB A:ADP409 3.3 48.3 0.8 O A:HOH548 3.5 49.7 1.0 O3A A:ADP409 3.6 0.7 0.8 O1B A:ADP409 3.8 48.3 0.8 CA A:GLY202 3.8 37.2 1.0 NZ A:LYS85 4.1 48.4 1.0 N A:GLY202 4.1 34.0 1.0 CD1 A:PHE67 4.3 68.7 0.5 C A:GLY202 4.3 37.7 1.0 CB A:ASP200 4.4 38.5 1.0 N A:SER203 4.6 34.3 1.0 OG A:SER203 4.6 40.2 1.0 CB A:PHE67 4.6 65.2 0.5 O2B A:ADP409 4.7 52.8 0.8 O A:HOH584 4.7 51.4 1.0 CG A:PHE67 4.7 68.0 0.5 MG A:MG405 4.8 51.1 1.0 OD2 A:ASP181 4.8 36.3 1.0 O A:GLY202 4.9 37.7 1.0

J.L.Stamos, M.L.Chu, M.D.Enos, N.Shah, W.I.Weis. Structural Basis of Gsk-3 Inhibition By N-Terminal Phosphorylation and By the Wnt Receptor LRP6. Elife V. 3 01998 2014.
ISSN: ESSN 2050-084X
PubMed: 24642411