Magnesium in PDB 4dg0: Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp

All present enzymatic activity of Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp:
2.7.11.11;

The structure of Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp, PDB code: 4dg0 was solved by A.C.Bastidas, J.M.Steichen, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.37 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.800, 78.730, 99.000, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.8

The binding sites of Magnesium atom in the Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp (pdb code 4dg0). 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 Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp, PDB code: 4dg0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp


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 Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg403 b:17.4 occ:1.00 O3G E:ANP402 1.9 22.9 1.0 O E:HOH597 2.0 18.9 1.0 O1B E:ANP402 2.0 22.0 1.0 O E:HOH598 2.3 13.0 1.0 OD1 E:ASP184 2.3 15.1 1.0 OD2 E:ASP184 2.4 15.5 1.0 CG E:ASP184 2.7 15.0 1.0 PG E:ANP402 3.1 22.4 1.0 PB E:ANP402 3.2 20.7 1.0 N3B E:ANP402 3.4 20.6 1.0 O2G E:ANP402 3.6 20.4 1.0 O I:HOH129 3.9 33.4 1.0 O E:HOH749 3.9 27.9 1.0 MG E:MG404 4.0 14.5 1.0 OG I:SER21 4.0 22.9 1.0 OD2 E:ASP166 4.1 15.1 1.0 CB E:ASP184 4.2 13.9 1.0 O2B E:ANP402 4.2 23.1 1.0 NZ E:LYS72 4.3 15.6 1.0 O1G E:ANP402 4.4 23.8 1.0 O3A E:ANP402 4.4 19.1 1.0 CA E:GLY186 4.4 14.4 1.0 CB I:SER21 4.6 21.9 1.0 O2A E:ANP402 4.6 16.7 1.0 N E:GLY186 4.6 14.1 1.0 PA E:ANP402 4.8 17.0 1.0 O E:HOH748 4.8 39.9 1.0 O1A E:ANP402 4.9 17.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp


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 Myristoylated Wt Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg404 b:14.5 occ:1.00 O2G E:ANP402 1.9 20.4 1.0 O2A E:ANP402 2.1 16.7 1.0 OD1 E:ASN171 2.2 13.1 1.0 O E:HOH599 2.2 15.3 1.0 OD2 E:ASP184 2.3 15.5 1.0 N3B E:ANP402 2.5 20.6 1.0 PG E:ANP402 2.7 22.4 1.0 CG E:ASN171 3.2 13.1 1.0 CG E:ASP184 3.3 15.0 1.0 PA E:ANP402 3.4 17.0 1.0 PB E:ANP402 3.5 20.7 1.0 ND2 E:ASN171 3.5 13.2 1.0 O3G E:ANP402 3.6 22.9 1.0 CB E:ASP184 3.7 13.9 1.0 O1B E:ANP402 3.8 22.0 1.0 O3A E:ANP402 3.8 19.1 1.0 O1G E:ANP402 3.9 23.8 1.0 MG E:MG403 4.0 17.4 1.0 CE E:LYS168 4.1 12.7 1.0 O I:HOH102 4.2 16.3 1.0 OD1 E:ASP184 4.3 15.1 1.0 O E:HOH523 4.4 26.2 1.0 O1A E:ANP402 4.4 17.6 1.0 NZ E:LYS168 4.4 13.5 1.0 O5' E:ANP402 4.5 17.5 1.0 OD2 E:ASP166 4.5 15.1 1.0 O3' E:ANP402 4.5 16.6 1.0 CB E:ASN171 4.5 13.4 1.0 C5' E:ANP402 4.7 17.4 1.0 O E:HOH522 4.8 24.9 1.0 CA E:ASN171 4.8 13.5 1.0 O2B E:ANP402 4.8 23.1 1.0 O E:HOH598 4.9 13.0 1.0 O E:GLU170 5.0 14.3 1.0 C3' E:ANP402 5.0 16.1 1.0

A.C.Bastidas, M.S.Deal, J.M.Steichen, M.M.Keshwani, Y.Guo, S.S.Taylor. Role of N-Terminal Myristylation in the Structure and Regulation of Camp-Dependent Protein Kinase. J.Mol.Biol. V. 422 215 2012.
ISSN: ISSN 0022-2836
PubMed: 22617327
DOI: 10.1016/J.JMB.2012.05.021