Magnesium in PDB 5ng0: Structure of RIP2K(L294F) with Bound Amppcp

All present enzymatic activity of Structure of RIP2K(L294F) with Bound Amppcp:
2.7.10.2; 2.7.11.1;

The structure of Structure of RIP2K(L294F) with Bound Amppcp, PDB code: 5ng0 was solved by E.Pellegrini, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.180, 94.180, 201.250, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.1

The structure of Structure of RIP2K(L294F) with Bound Amppcp also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Magnesium atom in the Structure of RIP2K(L294F) with Bound Amppcp (pdb code 5ng0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of RIP2K(L294F) with Bound Amppcp, PDB code: 5ng0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of RIP2K(L294F) with Bound Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of RIP2K(L294F) with Bound Amppcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:42.5 occ:0.80 O A:HOH1259 2.2 47.4 1.0 O1G A:ACP1000 2.2 45.4 0.8 O1B A:ACP1000 2.2 43.8 0.8 OD2 A:ASP164 2.2 36.8 1.0 O A:HOH1153 2.2 39.1 1.0 OD1 A:ASP164 2.2 36.4 1.0 CG A:ASP164 2.5 33.6 1.0 O A:HOH1114 3.5 45.8 1.0 PB A:ACP1000 3.5 46.7 0.8 PG A:ACP1000 3.6 51.8 0.8 OD2 A:ASP146 3.9 36.2 1.0 O A:HOH1148 3.9 50.3 1.0 C3B A:ACP1000 4.0 48.2 0.8 CB A:ASP164 4.1 30.7 1.0 O A:HOH1231 4.1 49.2 1.0 NZ A:LYS47 4.3 43.1 1.0 O2G A:ACP1000 4.3 47.7 0.8 O2B A:ACP1000 4.4 47.5 0.8 O1A A:ACP1000 4.4 41.7 0.8 O3A A:ACP1000 4.6 46.8 0.8 O3G A:ACP1000 4.6 51.7 0.8 CA A:GLY166 4.7 33.3 1.0 N A:GLY166 4.8 32.0 1.0 CA A:ASP164 4.9 29.6 1.0 PA A:ACP1000 4.9 46.6 0.8 O A:ASP164 5.0 28.6 1.0

Magnesium binding site 2 out of 2 in the Structure of RIP2K(L294F) with Bound Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of RIP2K(L294F) with Bound Amppcp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:39.4 occ:0.80 O2G B:ACP401 2.2 45.0 0.8 O2B B:ACP401 2.2 42.4 0.8 O B:HOH647 2.2 44.5 1.0 OD2 B:ASP164 2.2 35.4 1.0 OD1 B:ASP164 2.2 33.5 1.0 O B:HOH511 2.2 36.9 1.0 CG B:ASP164 2.5 31.6 1.0 PG B:ACP401 3.4 48.0 0.8 PB B:ACP401 3.4 42.1 0.8 C3B B:ACP401 3.8 43.2 0.8 O B:HOH604 4.0 48.4 1.0 OD2 B:ASP146 4.0 32.4 1.0 O B:HOH514 4.0 46.0 1.0 CB B:ASP164 4.0 29.5 1.0 O1G B:ACP401 4.1 49.9 0.8 O B:HOH622 4.2 45.7 1.0 O1B B:ACP401 4.3 40.6 0.8 NZ B:LYS47 4.3 39.5 1.0 O2A B:ACP401 4.4 37.8 0.8 O3G B:ACP401 4.5 48.2 0.8 O3A B:ACP401 4.5 41.4 0.8 CA B:GLY166 4.7 26.9 1.0 N B:GLY166 4.8 27.7 1.0 PA B:ACP401 4.8 39.8 0.8 CA B:ASP164 4.9 27.2 1.0 O1A B:ACP401 4.9 38.2 0.8 O B:ASP164 5.0 25.9 1.0

E.Pellegrini, L.Signor, S.Singh, E.Boeri Erba, S.Cusack. Structures of the Inactive and Active States of RIP2 Kinase Inform on the Mechanism of Activation. Plos One V. 12 77161 2017.
ISSN: ESSN 1932-6203
PubMed: 28545134
DOI: 10.1371/JOURNAL.PONE.0177161