Magnesium in PDB 3uds: Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp.

All present enzymatic activity of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp.:
2.7.1.158;

The structure of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp., PDB code: 3uds was solved by V.Gosein, T.-F.Leung, O.Krajden, G.J.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.82 / 3.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	58.289, 59.877, 82.913, 83.40, 89.40, 65.30
R / Rfree (%)	23.7 / 31.2

The binding sites of Magnesium atom in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp. (pdb code 3uds). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp., PDB code: 3uds:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg700 b:46.5 occ:1.00 OD2 A:ASP407 2.2 55.8 1.0 O2B A:ADP600 2.4 63.1 1.0 O1A A:ADP600 2.6 54.9 1.0 CG A:ASP407 3.5 52.5 1.0 PB A:ADP600 3.8 58.4 1.0 PA A:ADP600 3.9 50.7 1.0 O3A A:ADP600 4.2 56.9 1.0 O3' A:ADP600 4.2 51.7 1.0 CB A:ASP407 4.3 45.3 1.0 OG A:SER370 4.3 49.9 1.0 CA A:GLY19 4.4 60.2 1.0 OD1 A:ASP407 4.4 49.6 1.0 O1B A:ADP600 4.4 54.0 1.0 CD A:LYS168 4.7 41.8 1.0 O5' A:ADP600 4.9 53.8 1.0 C5' A:ADP600 4.9 52.1 1.0 N A:GLY19 4.9 56.6 1.0 O3B A:ADP600 4.9 60.7 1.0

Magnesium binding site 2 out of 2 in the Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase From A. Thaliana in Complex with Adp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg700 b:64.7 occ:1.00 OD2 B:ASP407 2.2 72.3 1.0 O2B B:ADP600 2.8 73.1 1.0 O1A B:ADP600 3.2 77.3 1.0 CG B:ASP407 3.4 74.3 1.0 O5' B:ADP600 3.9 79.1 1.0 O3' B:ADP600 4.0 58.5 1.0 PA B:ADP600 4.0 77.5 1.0 PB B:ADP600 4.1 74.4 1.0 CB B:ASP407 4.1 67.4 1.0 O3A B:ADP600 4.2 78.8 1.0 OD1 B:ASP407 4.3 73.1 1.0 OG B:SER370 4.3 60.2 1.0 C3' B:ADP600 4.6 68.6 1.0 CA B:GLY19 4.6 82.0 1.0 OE2 B:GLU166 4.6 63.1 1.0 C5' B:ADP600 4.8 76.1 1.0 N B:GLY20 4.8 91.5 1.0 O1B B:ADP600 4.9 75.0 1.0

V.Gosein, T.F.Leung, O.Krajden, G.J.Miller. Inositol Phosphate-Induced Stabilization of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinase and Its Role in Substrate Specificity. Protein Sci. V. 21 737 2012.
ISSN: ISSN 0961-8368
PubMed: 22362712
DOI: 10.1002/PRO.2049