Magnesium in PDB 8c08: Crystal Structure of JAK2 JH2-K539L

All present enzymatic activity of Crystal Structure of JAK2 JH2-K539L:
2.7.10.2;

The structure of Crystal Structure of JAK2 JH2-K539L, PDB code: 8c08 was solved by T.Haikarainen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	77.37 / 2.20
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	46.857, 46.857, 309.461, 90, 90, 90
R / Rfree (%)	23 / 25.9

The binding sites of Magnesium atom in the Crystal Structure of JAK2 JH2-K539L (pdb code 8c08). 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 JAK2 JH2-K539L, PDB code: 8c08:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of JAK2 JH2-K539L


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 JAK2 JH2-K539L within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:39.7 occ:1.00 O A:HOH1004 2.2 39.8 1.0 O2B A:ATP901 2.2 54.3 1.0 O1G A:ATP901 2.5 50.5 1.0 O2A A:ATP901 2.7 51.2 1.0 OD1 A:ASN678 2.8 45.4 1.0 HG A:SER698 2.8 70.8 1.0 CG A:ASN678 3.2 43.4 1.0 HD21 A:ASN678 3.2 48.5 1.0 PB A:ATP901 3.3 41.4 1.0 O3B A:ATP901 3.3 52.9 1.0 O A:HOH1017 3.4 53.8 1.0 ND2 A:ASN678 3.4 40.3 1.0 PG A:ATP901 3.4 52.8 1.0 OG A:SER698 3.4 59.0 1.0 HZ2 A:LYS581 3.5 59.6 1.0 O3A A:ATP901 3.6 25.6 1.0 PA A:ATP901 3.8 49.4 1.0 HA A:ASN678 3.8 49.4 1.0 HE3 A:LYS677 3.9 60.6 1.0 O A:ASP699 3.9 50.2 1.0 HZ3 A:LYS581 4.0 59.6 1.0 HD22 A:ASN678 4.1 48.5 1.0 NZ A:LYS581 4.2 49.6 1.0 O3G A:ATP901 4.2 37.3 1.0 CB A:ASN678 4.2 39.6 1.0 OD1 A:ASP699 4.3 45.4 1.0 HB3 A:ASN678 4.3 47.6 1.0 HB2 A:SER698 4.4 60.0 1.0 HE3 A:LYS581 4.5 65.9 1.0 CB A:SER698 4.5 49.9 1.0 CA A:ASN678 4.5 41.0 1.0 O1A A:ATP901 4.6 52.5 1.0 O1B A:ATP901 4.6 45.4 1.0 HZ1 A:LYS677 4.7 65.9 1.0 HD22 A:ASN673 4.7 61.8 1.0 O2G A:ATP901 4.7 52.8 1.0 HZ2 A:LYS677 4.8 65.9 1.0 CE A:LYS677 4.8 50.4 1.0 HA3 A:GLY701 4.8 58.1 1.0 HD21 A:ASN673 4.8 61.8 1.0 HZ1 A:LYS581 4.8 59.6 1.0 CE A:LYS581 4.9 54.8 1.0 HB3 A:SER698 4.9 60.0 1.0 H8 A:ATP901 5.0 50.9 1.0 HG2 A:LYS677 5.0 66.5 1.0 O5' A:ATP901 5.0 41.4 1.0 NZ A:LYS677 5.0 54.8 1.0 ND2 A:ASN673 5.0 51.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of JAK2 JH2-K539L


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 JAK2 JH2-K539L within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg903 b:44.7 occ:1.00 O B:HOH1040 2.0 43.5 1.0 O B:HOH1033 2.2 40.7 1.0 O2A B:ATP901 2.4 47.9 1.0 OD1 B:ASN678 2.4 56.4 1.0 O3G B:ATP901 2.8 54.5 1.0 O2B B:ATP901 2.8 55.2 1.0 HG B:SER698 2.9 66.8 1.0 CG B:ASN678 3.0 47.6 1.0 HZ1 B:LYS581 3.3 61.9 1.0 HE3 B:LYS677 3.3 58.4 1.0 HD21 B:ASN678 3.3 56.8 1.0 O3B B:ATP901 3.3 52.6 1.0 O B:HOH1023 3.4 41.4 1.0 HA B:ASN678 3.4 54.6 1.0 ND2 B:ASN678 3.4 47.3 1.0 PB B:ATP901 3.5 54.0 1.0 O3A B:ATP901 3.5 35.7 1.0 HZ3 B:LYS581 3.6 61.9 1.0 PA B:ATP901 3.6 46.3 1.0 PG B:ATP901 3.6 57.3 1.0 OG B:SER698 3.7 55.6 1.0 NZ B:LYS581 3.9 51.5 1.0 CB B:ASN678 4.0 45.6 1.0 HD22 B:ASN678 4.1 56.8 1.0 O2G B:ATP901 4.1 43.2 1.0 CA B:ASN678 4.1 45.4 1.0 HB2 B:SER698 4.2 56.3 1.0 CE B:LYS677 4.3 48.6 1.0 HB3 B:ASN678 4.3 54.9 1.0 CB B:SER698 4.4 46.9 1.0 HG2 B:LYS677 4.4 73.3 1.0 HZ2 B:LYS581 4.4 61.9 1.0 H8 B:ATP901 4.5 55.0 1.0 HB3 B:SER698 4.5 56.3 1.0 O1A B:ATP901 4.5 60.0 1.0 HE2 B:LYS581 4.6 63.5 1.0 HZ1 B:LYS677 4.6 66.7 1.0 HE2 B:LYS677 4.6 58.4 1.0 O5' B:ATP901 4.6 42.2 1.0 HZ2 B:LYS677 4.7 66.7 1.0 N B:ASN678 4.8 46.9 1.0 NZ B:LYS677 4.8 55.5 1.0 CE B:LYS581 4.8 52.8 1.0 HB2 B:ASN678 4.9 54.9 1.0 O1B B:ATP901 4.9 57.0 1.0 O1G B:ATP901 5.0 65.7 1.0 OD1 B:ASP699 5.0 37.4 1.0 H5'1 B:ATP901 5.0 62.9 1.0

B.G.Abraham, T.Haikarainen, J.Vuorio, M.Girych, A.Virtanen, V.Sharma, I.Vattulainen, O.Silvennoinen. Erythropoietin Signaling Is Mediated By Receptor Dimerization Through JAK2 Pseudokinase Domain To Be Published.