Magnesium in PDB 3ohm: Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3

Enzymatic activity of Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3

All present enzymatic activity of Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3:
3.1.4.11;

Protein crystallography data

The structure of Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3, PDB code: 3ohm was solved by G.L.Waldo, J.Sondek, T.K.Harden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 202.988, 90.881, 93.140, 90.00, 101.16, 90.00
R / Rfree (%) 20.4 / 27.5

Other elements in 3ohm:

The structure of Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3 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 Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3 (pdb code 3ohm). 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 Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3, PDB code: 3ohm:

Magnesium binding site 1 out of 1 in 3ohm

Go back to Magnesium Binding Sites List in 3ohm
Magnesium binding site 1 out of 1 in the Crystal Structure of Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3


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 Activated G Alpha Q Bound to Its Effector Phospholipase C Beta 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:52.9
occ:1.00
 O2B A:GDP400 1.9 43.6 1.0
OG A:SER53 2.0 53.5 1.0
OG1 A:THR186 2.1 53.9 1.0
O A:HOH436 2.2 48.9 1.0
F3 A:ALF401 2.3 49.4 1.0
CB A:SER53 2.8 54.4 1.0
F1 A:ALF401 3.0 54.9 1.0
PB A:GDP400 3.1 50.8 1.0
O2A A:GDP400 3.3 42.0 1.0
O3B A:GDP400 3.3 48.6 1.0
CB A:THR186 3.4 54.5 1.0
AL A:ALF401 3.4 49.2 1.0
N A:SER53 3.8 54.0 1.0
O1A A:GDP400 3.8 44.1 1.0
CA A:SER53 3.9 54.4 1.0
PA A:GDP400 4.0 44.9 1.0
N A:THR186 4.0 53.7 1.0
O3A A:GDP400 4.0 46.7 1.0
CA A:THR186 4.3 54.4 1.0
OD2 A:ASP205 4.3 68.0 1.0
O A:HOH437 4.3 39.9 1.0
O A:VAL184 4.3 53.7 1.0
NH1 A:ARG183 4.4 56.0 1.0
CG2 A:THR186 4.4 52.4 1.0
O1B A:GDP400 4.4 47.0 1.0
O A:HOH388 4.5 51.8 1.0
OD1 A:ASP205 4.6 71.1 1.0
F2 A:ALF401 4.6 52.5 1.0
C A:PRO185 4.7 52.8 1.0
CG A:ASP205 4.9 67.7 1.0
C A:LYS52 5.0 53.0 1.0
F4 A:ALF401 5.0 48.1 1.0
CE A:LYS52 5.0 50.8 1.0

Reference:

G.L.Waldo, T.K.Ricks, S.N.Hicks, M.L.Cheever, T.Kawano, K.Tsuboi, X.Wang, C.Montell, T.Kozasa, J.Sondek, T.K.Harden. Kinetic Scaffolding Mediated By A Phospholipase C-{Beta} and Gq Signaling Complex. Science V. 330 974 2010.
ISSN: ISSN 0036-8075
PubMed: 20966218
DOI: 10.1126/SCIENCE.1193438
Page generated: Mon Dec 14 08:35:05 2020

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