Magnesium in PDB 4dfx: Crystal Structure of Myristoylated K7C Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp

All present enzymatic activity of Crystal Structure of Myristoylated K7C 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 K7C Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp, PDB code: 4dfx 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)	25.03 / 1.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.100, 79.700, 117.230, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 17.9

The binding sites of Magnesium atom in the Crystal Structure of Myristoylated K7C Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp (pdb code 4dfx). 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 K7C Catalytic Subunit of Camp- Dependent Protein Kinase in Complex with SP20 and Amp-Pnp, PDB code: 4dfx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Myristoylated K7C 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 K7C 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:8.2 occ:1.00 O2A E:ANP402 2.0 9.8 1.0 O2G E:ANP402 2.0 10.3 1.0 OD1 E:ASN171 2.0 8.6 1.0 O E:HOH520 2.1 13.3 1.0 OD2 E:ASP184 2.1 7.9 1.0 N3B E:ANP402 2.8 13.1 1.0 PG E:ANP402 2.9 10.6 1.0 CG E:ASN171 3.1 6.9 1.0 CG E:ASP184 3.1 8.1 1.0 PA E:ANP402 3.3 10.3 1.0 ND2 E:ASN171 3.5 8.2 1.0 CB E:ASP184 3.6 7.5 1.0 O3G E:ANP402 3.7 10.8 1.0 PB E:ANP402 3.7 10.8 1.0 O3A E:ANP402 3.8 11.2 1.0 MG E:MG404 3.8 9.4 1.0 O1B E:ANP402 3.9 10.2 1.0 CE E:LYS168 4.1 9.1 1.0 O1G E:ANP402 4.2 12.0 1.0 OD1 E:ASP184 4.2 9.0 1.0 O1A E:ANP402 4.2 10.6 1.0 O3' E:ANP402 4.3 10.0 1.0 NZ E:LYS168 4.3 9.8 1.0 O I:HOH101 4.4 14.4 1.0 O E:HOH594 4.4 15.7 1.0 O5' E:ANP402 4.4 9.8 1.0 CB E:ASN171 4.4 6.6 1.0 OD2 E:ASP166 4.5 9.5 1.0 C5' E:ANP402 4.6 10.2 1.0 CA E:ASN171 4.8 7.2 1.0 O E:HOH522 4.8 13.0 1.0 O E:GLU170 4.8 8.2 1.0 C3' E:ANP402 4.9 9.2 1.0 O E:HOH521 5.0 15.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Myristoylated K7C 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 K7C 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:9.4 occ:1.00 O3G E:ANP402 2.0 10.8 1.0 O E:HOH526 2.0 13.6 1.0 O1B E:ANP402 2.0 10.2 1.0 O E:HOH522 2.1 13.0 1.0 OD2 E:ASP184 2.2 7.9 1.0 OD1 E:ASP184 2.2 9.0 1.0 CG E:ASP184 2.5 8.1 1.0 PG E:ANP402 3.1 10.6 1.0 PB E:ANP402 3.2 10.8 1.0 N3B E:ANP402 3.4 13.1 1.0 O2G E:ANP402 3.6 10.3 1.0 MG E:MG403 3.8 8.2 1.0 O E:HOH525 4.0 19.6 1.0 OG I:SER21 4.0 12.5 1.0 CB E:ASP184 4.1 7.5 1.0 OD2 E:ASP166 4.1 9.5 1.0 O I:HOH123 4.2 26.7 1.0 O3A E:ANP402 4.3 11.2 1.0 NZ E:LYS72 4.3 10.8 1.0 O2B E:ANP402 4.3 12.7 1.0 O1G E:ANP402 4.4 12.0 1.0 O2A E:ANP402 4.5 9.8 1.0 CA E:GLY186 4.5 8.6 1.0 CB I:SER21 4.6 11.3 1.0 N E:GLY186 4.6 7.9 1.0 PA E:ANP402 4.7 10.3 1.0 O E:HOH776 4.7 49.1 1.0 O1A E:ANP402 4.8 10.6 1.0 CA E:ASP184 4.9 7.3 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