Magnesium in PDB 3qam: Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase

All present enzymatic activity of Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase:
2.7.11.11;

The structure of Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase, PDB code: 3qam was solved by J.Yang, J.Wu, J.Steichen, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.92
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.412, 79.639, 60.800, 90.00, 113.28, 90.00
R / Rfree (%)	19.5 / 22.8

The binding sites of Magnesium atom in the Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase (pdb code 3qam). 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 GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase, PDB code: 3qam:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase


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 GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg352 b:27.4 occ:1.00 O2A E:ATP351 2.0 24.1 1.0 OD1 E:ASN171 2.0 20.6 1.0 OD2 E:ASP184 2.1 20.4 1.0 O2G E:ATP351 2.2 21.2 1.0 O E:HOH414 2.2 22.8 1.0 O3B E:ATP351 2.5 25.0 1.0 PG E:ATP351 2.9 24.1 1.0 CG E:ASN171 3.0 25.8 1.0 CG E:ASP184 3.1 20.8 1.0 PA E:ATP351 3.3 25.4 1.0 ND2 E:ASN171 3.4 22.8 1.0 PB E:ATP351 3.5 24.9 1.0 CB E:ASP184 3.5 19.7 1.0 O1B E:ATP351 3.6 24.5 1.0 O3G E:ATP351 3.7 19.6 1.0 MG E:MG353 3.7 20.8 1.0 O3A E:ATP351 3.7 24.4 1.0 O1A E:ATP351 4.0 24.7 1.0 CE E:LYS168 4.1 21.2 1.0 O1G E:ATP351 4.1 20.3 1.0 OD1 E:ASP184 4.2 18.9 1.0 O3' E:ATP351 4.3 24.3 1.0 OD2 E:ASP166 4.3 26.5 1.0 NZ E:LYS168 4.3 19.5 1.0 CB E:ASN171 4.4 23.7 1.0 O I:HOH416 4.4 27.2 1.0 O5' E:ATP351 4.5 25.3 1.0 C5' E:ATP351 4.7 25.0 1.0 CA E:ASN171 4.8 23.2 1.0 O E:HOH415 4.8 20.8 1.0 O2B E:ATP351 4.8 28.2 1.0 C3' E:ATP351 4.9 26.2 1.0 O E:GLU170 5.0 23.7 1.0 CA E:ASP184 5.0 22.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase


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 GLU208ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg353 b:20.8 occ:1.00 O3G E:ATP351 2.0 19.6 1.0 O E:HOH415 2.1 20.8 1.0 O1B E:ATP351 2.1 24.5 1.0 OD2 E:ASP184 2.1 20.4 1.0 O E:HOH413 2.2 20.1 1.0 OD1 E:ASP184 2.2 18.9 1.0 CG E:ASP184 2.4 20.8 1.0 PG E:ATP351 3.0 24.1 1.0 PB E:ATP351 3.2 24.9 1.0 O2G E:ATP351 3.5 21.2 1.0 O3B E:ATP351 3.5 25.0 1.0 MG E:MG352 3.7 27.4 1.0 CD2 E:PHE54 3.9 47.1 1.0 CB E:ASP184 4.0 19.7 1.0 OD2 E:ASP166 4.0 26.5 1.0 O2B E:ATP351 4.0 28.2 1.0 O E:HOH412 4.2 24.3 1.0 CE2 E:PHE54 4.2 47.5 1.0 NZ E:LYS72 4.3 22.1 1.0 O1G E:ATP351 4.4 20.3 1.0 O2A E:ATP351 4.4 24.1 1.0 O3A E:ATP351 4.4 24.4 1.0 CA E:GLY186 4.4 23.6 1.0 O1A E:ATP351 4.5 24.7 1.0 N E:GLY186 4.6 23.2 1.0 PA E:ATP351 4.7 25.4 1.0 CB I:ALA21 4.8 22.4 1.0 CA E:ASP184 4.8 22.1 1.0 ND2 E:ASN171 4.8 22.8 1.0 O E:ASP184 4.9 22.8 1.0 C E:ASP184 5.0 23.2 1.0

J.Yang, J.Wu, J.M.Steichen, A.P.Kornev, M.S.Deal, S.Li, B.Sankaran, V.L.Woods, S.S.Taylor. A Conserved Glu-Arg Salt Bridge Connects Coevolved Motifs That Define the Eukaryotic Protein Kinase Fold. J.Mol.Biol. V. 415 666 2012.
ISSN: ISSN 0022-2836
PubMed: 22138346
DOI: 10.1016/J.JMB.2011.11.035