Magnesium in PDB 4gnk: Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3

All present enzymatic activity of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3:
3.1.4.11;

The structure of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3, PDB code: 4gnk was solved by A.M.Lyon, J.J.G.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 4.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.423, 188.845, 293.857, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 25.5

The structure of Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Aluminium	(Al)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3 (pdb code 4gnk). 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 Galphaq in Complex with Full-Length Human PLCBETA3, PDB code: 4gnk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3


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 Galphaq in Complex with Full-Length Human PLCBETA3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:96.1 occ:1.00 F3 A:ALF402 2.0 93.0 1.0 O A:HOH503 2.1 96.2 1.0 O A:HOH502 2.1 98.4 1.0 O2B A:GDP401 2.2 93.4 1.0 OG A:SER53 2.2 99.0 1.0 OG1 A:THR186 2.2 0.0 1.0 O3B A:GDP401 2.7 94.1 1.0 PB A:GDP401 2.9 94.1 1.0 CB A:THR186 3.1 0.6 1.0 AL A:ALF402 3.1 93.4 1.0 CB A:SER53 3.2 0.2 1.0 F2 A:ALF402 3.4 95.0 1.0 N A:SER53 3.7 98.9 1.0 N A:THR186 3.7 0.8 1.0 F4 A:ALF402 3.9 95.8 1.0 O3A A:GDP401 4.0 94.8 1.0 O2A A:GDP401 4.0 94.2 1.0 O1A A:GDP401 4.0 97.0 1.0 CA A:THR186 4.0 0.8 1.0 CA A:SER53 4.1 0.2 1.0 O1B A:GDP401 4.1 94.2 1.0 PA A:GDP401 4.1 95.8 1.0 CG2 A:THR186 4.3 0.9 1.0 OD2 A:ASP205 4.3 0.6 1.0 OD1 A:ASP205 4.4 0.1 1.0 O A:HOH501 4.4 92.1 1.0 O A:VAL206 4.6 94.5 1.0 CB A:LYS52 4.6 0.8 1.0 F1 A:ALF402 4.7 95.6 1.0 C A:LYS52 4.7 0.6 1.0 CG A:ASP205 4.8 0.0 1.0 C A:PRO185 4.9 98.9 1.0 O A:VAL184 4.9 92.2 1.0 C A:THR186 5.0 99.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Galphaq in Complex with Full-Length Human PLCBETA3


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 Galphaq in Complex with Full-Length Human PLCBETA3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg403 b:87.5 occ:1.00 O2B C:GDP401 1.8 87.0 1.0 F3 C:ALF402 2.0 85.3 1.0 OG C:SER53 2.0 96.9 1.0 O C:HOH502 2.1 85.1 1.0 O C:HOH503 2.1 89.9 1.0 OG1 C:THR186 2.2 99.5 1.0 PB C:GDP401 2.9 87.5 1.0 O3B C:GDP401 3.0 87.1 1.0 CB C:THR186 3.2 96.8 1.0 CB C:SER53 3.2 99.5 1.0 AL C:ALF402 3.3 82.4 1.0 F2 C:ALF402 3.5 85.1 1.0 N C:SER53 3.7 0.9 1.0 N C:THR186 3.7 92.7 1.0 O2A C:GDP401 3.8 83.0 1.0 O3A C:GDP401 3.9 86.5 1.0 F4 C:ALF402 4.0 83.8 1.0 CA C:SER53 4.0 0.2 1.0 O1B C:GDP401 4.0 86.4 1.0 CA C:THR186 4.1 94.5 1.0 PA C:GDP401 4.1 84.5 1.0 O1A C:GDP401 4.1 86.2 1.0 OD2 C:ASP205 4.2 96.2 1.0 CG2 C:THR186 4.3 97.9 1.0 OD1 C:ASP205 4.4 98.4 1.0 O C:VAL206 4.5 84.1 1.0 O C:HOH501 4.5 82.4 1.0 CB C:LYS52 4.6 0.3 1.0 C C:LYS52 4.7 0.9 1.0 CG C:ASP205 4.8 97.6 1.0 O C:VAL184 4.8 96.2 1.0 C C:PRO185 4.9 91.9 1.0 F1 C:ALF402 5.0 82.8 1.0 CE C:LYS52 5.0 0.9 1.0 N C:LYS52 5.0 0.7 1.0

A.M.Lyon, S.Dutta, C.A.Boguth, G.Skiniotis, J.J.Tesmer. Full-Length G Alpha (Q)-Phospholipase C-Beta 3 Structure Reveals Interfaces of the C-Terminal Coiled-Coil Domain. Nat.Struct.Mol.Biol. V. 20 355 2013.
ISSN: ISSN 1545-9993
PubMed: 23377541
DOI: 10.1038/NSMB.2497