Magnesium in PDB 3x2u: Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit.

All present enzymatic activity of Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit.:
2.7.11.11;

The structure of Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit., PDB code: 3x2u was solved by A.Das, P.Langan, O.Gerlits, A.Y.Kovalevsky, W.T.Heller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.95 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.660, 74.680, 79.910, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 23.9

The binding sites of Magnesium atom in the Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit. (pdb code 3x2u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit., PDB code: 3x2u:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:63.4 occ:0.90 O3G A:ATP501 1.9 71.4 0.9 OD2 A:ASP184 1.9 55.1 1.0 O A:HOH649 2.1 52.2 1.0 O1B A:ATP501 2.3 60.7 0.9 OD1 A:ASP184 2.4 49.2 1.0 CG A:ASP184 2.4 49.0 1.0 PG A:ATP501 2.7 87.4 0.9 O2G A:ATP501 2.9 68.7 0.9 O3B A:ATP501 3.0 62.1 0.9 PB A:ATP501 3.2 73.3 0.9 O A:HOH777 3.7 43.1 0.8 O2A A:ATP501 3.8 57.0 0.9 MG A:MG503 3.8 50.6 0.5 CB A:ASP184 3.9 39.3 1.0 O3A A:ATP501 4.1 67.2 0.9 O1G A:ATP501 4.1 64.9 0.9 PA A:ATP501 4.3 63.7 0.9 OG S:SER621 4.5 54.9 1.0 O1A A:ATP501 4.5 55.6 0.9 O2B A:ATP501 4.5 65.9 0.9 NZ A:LYS72 4.7 55.1 1.0 O A:HOH693 4.8 50.5 1.0 CA A:GLY186 4.8 33.3 1.0 CA A:ASP184 4.8 41.8 1.0 N A:GLY186 4.8 35.7 1.0 OD2 A:ASP166 5.0 43.8 1.0

Magnesium binding site 2 out of 2 in the Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Michaelis-Like Initial Complex of Camp-Dependent Protein Kinase Catalytic Subunit. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:50.6 occ:0.50 O2A A:ATP501 2.0 57.0 0.9 O2G A:ATP501 2.2 68.7 0.9 OD1 A:ASN171 2.3 37.2 1.0 O A:HOH607 2.3 48.9 1.0 OD2 A:ASP184 2.5 55.1 1.0 O3B A:ATP501 2.7 62.1 0.9 PG A:ATP501 3.1 87.4 0.9 CG A:ASN171 3.2 41.7 1.0 CG A:ASP184 3.3 49.0 1.0 PA A:ATP501 3.4 63.7 0.9 ND2 A:ASN171 3.4 36.8 1.0 CB A:ASP184 3.6 39.3 1.0 MG A:MG502 3.8 63.4 0.9 PB A:ATP501 3.9 73.3 0.9 O3A A:ATP501 3.9 67.2 0.9 O1G A:ATP501 4.1 64.9 0.9 O3G A:ATP501 4.1 71.4 0.9 O1A A:ATP501 4.2 55.6 0.9 O5' A:ATP501 4.3 54.5 0.9 CE A:LYS168 4.3 32.9 1.0 OD1 A:ASP184 4.4 49.2 1.0 O1B A:ATP501 4.4 60.7 0.9 C5' A:ATP501 4.5 51.6 0.9 O A:HOH602 4.6 53.6 1.0 CB A:ASN171 4.6 38.9 1.0 NZ A:LYS168 4.6 37.4 1.0 OG S:SER621 4.7 54.9 1.0 OD2 A:ASP166 4.9 43.8 1.0 O A:HOH649 5.0 52.2 1.0

A.Das, O.Gerlits, J.M.Parks, P.Langan, A.Kovalevsky, W.T.Heller. Protein Kinase A Catalytic Subunit Primed For Action: Time-Lapse Crystallography of Michaelis Complex Formation. Structure V. 23 2331 2015.
ISSN: ISSN 0969-2126
PubMed: 26585512
DOI: 10.1016/J.STR.2015.10.005