Magnesium in PDB 4dg3: Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif.

All present enzymatic activity of Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif.:
2.7.11.11;

The structure of Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif., PDB code: 4dg3 was solved by J.M.Steichen, J.Yang, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.34 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.290, 76.690, 80.310, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.7

The binding sites of Magnesium atom in the Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif. (pdb code 4dg3). 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 R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif., PDB code: 4dg3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif.


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 R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif. within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg402 b:17.4 occ:1.00 O2A E:ANP401 2.0 17.8 1.0 OD1 E:ASN171 2.0 16.5 1.0 O E:HOH715 2.1 16.6 1.0 O2G E:ANP401 2.1 17.7 1.0 OD2 E:ASP184 2.1 16.6 1.0 N3B E:ANP401 2.6 18.2 1.0 PG E:ANP401 2.9 18.9 1.0 CG E:ASN171 3.0 16.8 1.0 CG E:ASP184 3.1 17.3 1.0 PA E:ANP401 3.3 19.6 1.0 ND2 E:ASN171 3.5 15.9 1.0 CB E:ASP184 3.6 17.3 1.0 PB E:ANP401 3.6 18.9 1.0 O3G E:ANP401 3.7 19.1 1.0 O3A E:ANP401 3.7 18.0 1.0 MG E:MG403 3.8 17.8 1.0 O1B E:ANP401 3.9 17.8 1.0 CE E:LYS168 4.0 16.3 1.0 O1G E:ANP401 4.1 20.1 1.0 OD1 E:ASP184 4.2 16.9 1.0 O1A E:ANP401 4.3 19.4 1.0 NZ E:LYS168 4.3 16.3 1.0 O3' E:ANP401 4.4 20.2 1.0 O5' E:ANP401 4.4 19.7 1.0 CB E:ASN171 4.4 17.0 1.0 O A:HOH107 4.4 19.1 1.0 OD2 E:ASP166 4.4 18.5 1.0 O A:HOH108 4.4 22.9 1.0 C5' E:ANP401 4.5 19.3 1.0 O E:HOH694 4.7 19.5 1.0 CA E:ASN171 4.7 17.8 1.0 C3' E:ANP401 4.8 19.8 1.0 O E:GLU170 4.8 17.9 1.0 N E:ASN171 5.0 17.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif.


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 R336A Mutant of Camp-Dependent Protein Kinase with Unphosphorylated Turn Motif. within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg403 b:17.8 occ:1.00 O E:HOH701 2.0 15.7 1.0 O3G E:ANP401 2.0 19.1 1.0 O1B E:ANP401 2.0 17.8 1.0 O E:HOH694 2.1 19.5 1.0 OD2 E:ASP184 2.2 16.6 1.0 OD1 E:ASP184 2.2 16.9 1.0 CG E:ASP184 2.5 17.3 1.0 PG E:ANP401 3.1 18.9 1.0 PB E:ANP401 3.2 18.9 1.0 N3B E:ANP401 3.5 18.2 1.0 O2G E:ANP401 3.7 17.7 1.0 O E:HOH509 3.8 42.8 1.0 MG E:MG402 3.8 17.4 1.0 OD2 E:ASP166 4.0 18.5 1.0 CB E:ASP184 4.0 17.3 1.0 O E:HOH712 4.2 23.2 1.0 NZ E:LYS72 4.2 19.1 1.0 O2B E:ANP401 4.3 18.9 1.0 O3A E:ANP401 4.3 18.0 1.0 CA E:GLY186 4.4 18.0 1.0 O1G E:ANP401 4.4 20.1 1.0 O2A E:ANP401 4.5 17.8 1.0 N E:GLY186 4.6 17.2 1.0 PA E:ANP401 4.7 19.6 1.0 CB A:ALA21 4.7 20.4 1.0 O1A E:ANP401 4.8 19.4 1.0 CA E:ASP184 4.9 17.9 1.0 ND2 E:ASN171 5.0 15.9 1.0

J.M.Steichen, J.Yang, S.S.Taylor. Turn Motif Phosphorylation Regulates Processing of Camp-Dependent Protein Kinase To Be Published.