Magnesium in PDB 6em6: Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp

All present enzymatic activity of Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp:
2.7.11.11;

The structure of Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp, PDB code: 6em6 was solved by J.M.Mueller, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.38 / 1.64
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.439, 73.162, 77.037, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 19.1

The binding sites of Magnesium atom in the Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp (pdb code 6em6). 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 the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp, PDB code: 6em6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp


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 the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:22.1 occ:1.00 O A:HOH609 1.9 22.4 1.0 O A:HOH657 2.0 24.0 1.0 O A:HOH630 2.0 26.0 1.0 O3B A:ADP401 2.1 22.5 1.0 OG A:SER53 2.1 26.9 1.0 O A:HOH549 2.1 20.8 1.0 HB2 A:SER53 3.1 32.8 1.0 CB A:SER53 3.1 27.3 1.0 PB A:ADP401 3.3 23.4 1.0 HB3 A:SER53 3.5 32.8 1.0 O1B A:ADP401 3.8 21.3 1.0 O A:HOH511 3.9 19.7 1.0 O2B A:ADP401 3.9 24.1 1.0 H A:SER53 4.0 32.6 1.0 OD1 A:ASP184 4.1 19.1 1.0 O A:HOH524 4.2 29.4 1.0 OD2 A:ASP184 4.2 19.7 1.0 O A:HOH688 4.2 26.5 1.0 HE1 A:PHE54 4.2 36.8 1.0 O A:HOH569 4.2 32.9 1.0 O A:HOH693 4.3 28.6 1.0 O A:HOH660 4.3 39.8 1.0 OE2 A:GLU91 4.4 18.6 1.0 CA A:SER53 4.4 28.0 1.0 HA3 A:GLY186 4.4 19.8 1.0 CG A:ASP184 4.5 19.4 1.0 O3A A:ADP401 4.5 21.6 1.0 N A:SER53 4.6 27.2 1.0 O A:HOH625 4.7 22.8 1.0 HA A:SER53 4.8 33.6 1.0 CE1 A:PHE54 4.8 30.7 1.0 HD1 A:PHE54 4.8 36.0 1.0 MG A:MG403 4.9 20.1 1.0 O A:HOH603 5.0 24.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp


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 the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP032 and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:20.1 occ:1.00 O1B A:ADP401 1.8 21.3 1.0 O A:HOH571 2.0 25.1 1.0 O A:HOH507 2.1 20.3 1.0 O A:HOH625 2.2 22.8 1.0 OD2 A:ASP184 2.2 19.7 1.0 O1A A:ADP401 2.2 22.5 1.0 PB A:ADP401 3.1 23.4 1.0 PA A:ADP401 3.3 20.1 1.0 CG A:ASP184 3.3 19.4 1.0 H5'1 A:ADP401 3.4 24.7 1.0 O3A A:ADP401 3.4 21.6 1.0 HB2 A:ASP184 3.6 22.2 1.0 O3B A:ADP401 3.8 22.5 1.0 O A:HOH609 3.8 22.4 1.0 O A:HOH537 3.8 31.9 1.0 O A:HOH509 3.9 30.0 1.0 CB A:ASP184 4.0 18.5 1.0 O C:HOH216 4.1 28.0 1.0 C5' A:ADP401 4.1 20.6 1.0 OD1 A:ASN171 4.2 17.1 1.0 O5' A:ADP401 4.2 20.7 1.0 H5'2 A:ADP401 4.3 24.7 1.0 O A:HOH514 4.3 20.9 1.0 OD1 A:ASP184 4.3 19.1 1.0 O2B A:ADP401 4.4 24.1 1.0 HB3 A:ASP184 4.4 22.2 1.0 O A:HOH524 4.4 29.4 1.0 O2A A:ADP401 4.5 18.6 1.0 O A:HOH671 4.6 26.7 1.0 OG A:SER53 4.9 26.9 1.0 MG A:MG402 4.9 22.1 1.0 HD21 A:ASN171 4.9 18.9 1.0

J.M.Mueller, R.Kirschner, A.Geyer, G.Klebe. Conceptional Design of Self-Assembling Bisubstrate-Like Inhibitors of Protein Kinase A Resulting in A Boronic Acid Glutamate Linkage Acs Omega 2019.
ISSN: ESSN 2470-1343
DOI: 10.1021/ACSOMEGA.8B02364