Magnesium in PDB 7tvf: Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom

All present enzymatic activity of Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom:
3.1.3.16; 3.6.5.2;

The structure of Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom, PDB code: 7tvf was solved by D.A.Bonsor, D.K.Simanshu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	101.70 / 2.17
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	129.938, 129.938, 326.795, 90, 90, 90
R / Rfree (%)	19.9 / 22.6

The structure of Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom also contains other interesting chemical elements:

Chlorine	(Cl)	5 atoms
Sodium	(Na)	2 atoms
Manganese	(Mn)	4 atoms

The binding sites of Magnesium atom in the Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom (pdb code 7tvf). 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 SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom, PDB code: 7tvf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom


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 SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg1205 b:39.9 occ:1.00 O3G E:GNP1201 2.0 41.2 1.0 OG1 E:THR45 2.1 38.4 1.0 O1B E:GNP1201 2.1 41.0 1.0 OG E:SER27 2.1 40.7 1.0 O E:HOH1305 2.1 41.4 1.0 O E:HOH1317 2.2 40.7 1.0 CB E:THR45 2.9 38.8 1.0 PG E:GNP1201 3.2 41.0 1.0 CB E:SER27 3.2 37.8 1.0 PB E:GNP1201 3.3 44.7 1.0 N3B E:GNP1201 3.6 42.2 1.0 O2G E:GNP1201 3.7 43.1 1.0 N E:THR45 3.8 39.8 1.0 OD2 E:ASP67 3.9 49.0 1.0 N E:SER27 3.9 41.1 1.0 CA E:THR45 3.9 38.5 1.0 CG2 E:THR45 4.0 40.1 1.0 CA E:SER27 4.1 43.3 1.0 OD1 E:ASP67 4.2 46.0 1.0 O2B E:GNP1201 4.3 41.3 1.0 O1A E:GNP1201 4.3 42.3 1.0 O E:HOH1315 4.4 44.3 1.0 O1G E:GNP1201 4.4 45.1 1.0 O3A E:GNP1201 4.4 39.6 1.0 CG E:ASP67 4.4 42.8 1.0 O E:THR68 4.4 36.5 1.0 O E:ASP43 4.5 48.3 1.0 O2A E:GNP1201 4.6 46.5 1.0 PA E:GNP1201 4.6 45.1 1.0 C E:PRO44 4.7 45.6 1.0 CB E:LYS26 4.8 38.1 1.0 C E:LYS26 4.9 40.3 1.0 CE E:LYS26 5.0 44.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom


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 SHOC2-Mras-PP1CA (Smp) Complex to A Resolution of 2.17 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1204 b:27.5 occ:1.00 O3G B:GNP1201 2.0 30.7 1.0 OG B:SER27 2.0 29.8 1.0 O1B B:GNP1201 2.0 29.7 1.0 O B:HOH1360 2.1 28.2 1.0 OG1 B:THR45 2.1 27.9 1.0 O B:HOH1324 2.1 28.9 1.0 CB B:THR45 3.0 28.0 1.0 CB B:SER27 3.1 31.1 1.0 PG B:GNP1201 3.2 30.9 1.0 PB B:GNP1201 3.3 31.9 1.0 N3B B:GNP1201 3.6 30.1 1.0 N B:THR45 3.8 29.4 1.0 O2G B:GNP1201 3.9 33.1 1.0 OD2 B:ASP67 3.9 34.0 1.0 N B:SER27 3.9 31.4 1.0 CA B:THR45 4.0 29.5 1.0 CG2 B:THR45 4.1 29.4 1.0 CA B:SER27 4.1 29.3 1.0 O1A B:GNP1201 4.2 35.0 1.0 OD1 B:ASP67 4.3 35.5 1.0 O2B B:GNP1201 4.3 34.8 1.0 O B:HOH1318 4.3 35.2 1.0 O3A B:GNP1201 4.4 32.2 1.0 O1G B:GNP1201 4.4 29.6 1.0 CG B:ASP67 4.5 31.8 1.0 O B:THR68 4.5 30.9 1.0 O B:ASP43 4.5 34.0 1.0 PA B:GNP1201 4.6 33.4 1.0 O2A B:GNP1201 4.6 33.3 1.0 C B:PRO44 4.8 33.6 1.0 O B:HOH1416 4.8 44.1 1.0 CB B:LYS26 4.9 27.0 1.0 C B:LYS26 4.9 31.2 1.0

D.A.Bonsor, P.Alexander, K.Snead, N.Hartig, M.Drew, S.Messing, L.I.Finci, D.V.Nissley, F.Mccormick, D.Esposito, P.Rodriguez-Viciana, A.G.Stephen, D.K.Simanshu. Structure of the SHOC2-Mras-PP1C Complex Provides Insights Into Raf Activation and Noonan Syndrome. Nat.Struct.Mol.Biol. V. 29 966 2022.
ISSN: ESSN 1545-9985
PubMed: 36175670
DOI: 10.1038/S41594-022-00841-4