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Magnesium in PDB 4qj3: Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

Enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq

All present enzymatic activity of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq:
3.1.4.11;

Protein crystallography data

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3 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) 29.71 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 200.623, 88.761, 92.232, 90.00, 101.39, 90.00
R / Rfree (%) 19.5 / 24

Other elements in 4qj3:

The structure of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Aluminium (Al) 1 atom
Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq (pdb code 4qj3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq, PDB code: 4qj3:

Magnesium binding site 1 out of 1 in 4qj3

Go back to Magnesium Binding Sites List in 4qj3
Magnesium binding site 1 out of 1 in the Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Fragment of Human Phospholipase C-BETA3 DELTA472-559, in Complex with Galphaq within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:32.8
occ:1.00
 OG A:SER53 2.2 33.7 1.0
OG1 A:THR186 2.2 36.1 1.0
O2B A:GDP400 2.2 30.9 1.0
F3 A:ALF401 2.3 30.9 1.0
O A:HOH508 2.7 16.3 1.0
F1 A:ALF401 2.8 30.8 1.0
CB A:SER53 3.1 33.8 1.0
PB A:GDP400 3.1 29.9 1.0
O3B A:GDP400 3.1 30.0 1.0
O2A A:GDP400 3.1 30.1 1.0
AL A:ALF401 3.3 30.6 1.0
CB A:THR186 3.3 37.4 1.0
N A:THR186 3.7 37.2 1.0
O A:VAL184 3.8 37.4 1.0
NH1 A:ARG183 3.8 36.5 1.0
O3A A:GDP400 3.8 29.4 1.0
PA A:GDP400 3.8 29.5 1.0
N A:SER53 4.1 33.6 1.0
CA A:THR186 4.1 37.9 1.0
O1A A:GDP400 4.1 30.0 1.0
CA A:SER53 4.2 34.1 1.0
O A:HOH501 4.4 18.1 1.0
O1B A:GDP400 4.4 29.9 1.0
CG2 A:THR186 4.5 38.5 1.0
F2 A:ALF401 4.5 31.2 1.0
C A:PRO185 4.6 37.8 1.0
OD2 A:ASP205 4.7 39.2 1.0
CA A:PRO185 4.8 37.2 1.0
F4 A:ALF401 4.8 30.1 1.0
C A:VAL184 4.8 37.3 1.0
CZ A:ARG183 4.9 36.4 1.0

Reference:

A.M.Lyon, J.A.Begley, T.Manett, J.J.G.Tesmer. Molecular Mechanisms of Plcbeta Regulation. Structure 2014.
ISSN: ISSN 0969-2126
Page generated: Tue Aug 20 02:00:40 2024

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