Magnesium in PDB 4dh7: Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20'

All present enzymatic activity of Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20':
2.7.11.11;

The structure of Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20', PDB code: 4dh7 was solved by A.Y.Kovalevsky, P.Langan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.535, 79.651, 98.011, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 19.4

The binding sites of Magnesium atom in the Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20' (pdb code 4dh7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20', PDB code: 4dh7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20'


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20' within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:18.3 occ:1.00 O3G A:ANP403 2.1 15.3 1.0 O A:HOH1003 2.1 16.1 1.0 O1B A:ANP403 2.1 15.4 1.0 O A:HOH1001 2.2 14.8 1.0 OD2 A:ASP184 2.2 16.0 1.0 OD1 A:ASP184 2.4 11.8 1.0 CG A:ASP184 2.6 14.5 1.0 PG A:ANP403 3.0 16.5 1.0 PB A:ANP403 3.2 17.6 1.0 N3B A:ANP403 3.5 15.0 1.0 O2G A:ANP403 3.5 14.8 1.0 MG A:MG402 3.8 18.0 1.0 OD2 A:ASP166 4.0 16.9 1.0 CD2 A:PHE54 4.0 22.3 1.0 O2B A:ANP403 4.1 17.3 1.0 CB A:ASP184 4.1 13.0 1.0 O A:HOH1038 4.3 17.6 1.0 CE2 A:PHE54 4.3 23.4 1.0 NZ A:LYS72 4.3 14.9 1.0 O2A A:ANP403 4.3 16.4 1.0 O1G A:ANP403 4.4 15.8 1.0 CA A:GLY186 4.4 14.8 1.0 O3A A:ANP403 4.4 16.4 1.0 N A:GLY186 4.6 13.5 1.0 CB I:ALA21 4.7 18.7 1.0 PA A:ANP403 4.7 16.5 1.0 O1A A:ANP403 4.7 16.6 1.0 CA A:ASP184 4.9 14.7 1.0 O A:HOH1065 5.0 22.0 1.0 ND2 A:ASN171 5.0 14.5 1.0

Magnesium binding site 2 out of 2 in the Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20'


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Low Temperature X-Ray Structure of Camp Dependent Protein Kinase A Catalytic Subunit with High MG2+, Amp-Pnp and IP20' within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:18.0 occ:1.00 O A:HOH1002 2.0 15.0 1.0 O2A A:ANP403 2.1 16.4 1.0 OD1 A:ASN171 2.1 14.7 1.0 OD2 A:ASP184 2.2 16.0 1.0 O2G A:ANP403 2.3 14.8 1.0 N3B A:ANP403 2.5 15.0 1.0 PG A:ANP403 2.9 16.5 1.0 CG A:ASN171 3.1 14.6 1.0 CG A:ASP184 3.2 14.5 1.0 PA A:ANP403 3.5 16.5 1.0 ND2 A:ASN171 3.5 14.5 1.0 PB A:ANP403 3.6 17.6 1.0 CB A:ASP184 3.7 13.0 1.0 O3G A:ANP403 3.8 15.3 1.0 MG A:MG401 3.8 18.3 1.0 O1B A:ANP403 3.9 15.4 1.0 O A:HOH1356 4.0 40.2 1.0 CE A:LYS168 4.0 13.8 1.0 O3A A:ANP403 4.0 16.4 1.0 O1G A:ANP403 4.1 15.8 1.0 NZ A:LYS168 4.3 13.8 1.0 OD1 A:ASP184 4.3 11.8 1.0 O3' A:ANP403 4.3 15.4 1.0 O1A A:ANP403 4.3 16.6 1.0 O I:HOH103 4.3 19.1 1.0 OD2 A:ASP166 4.4 16.9 1.0 O5' A:ANP403 4.5 16.8 1.0 CB A:ASN171 4.5 14.0 1.0 C5' A:ANP403 4.5 13.6 1.0 O A:HOH1003 4.8 16.1 1.0 CA A:ASN171 4.8 14.6 1.0 O A:GLU170 4.8 14.4 1.0 C3' A:ANP403 4.9 14.3 1.0 O2B A:ANP403 4.9 17.3 1.0

A.Y.Kovalevsky, H.Johnson, B.L.Hanson, M.J.Waltman, S.Z.Fisher, S.Taylor, P.Langan. Low- and Room-Temperature X-Ray Structures of Protein Kinase A Ternary Complexes Shed New Light on Its Activity. Acta Crystallogr.,Sect.D V. 68 854 2012.
ISSN: ISSN 0907-4449
PubMed: 22751671
DOI: 10.1107/S0907444912014886