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Magnesium in PDB 1svk: Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp

Enzymatic activity of Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp

All present enzymatic activity of Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp:
3.6.1.46;

Protein crystallography data

The structure of Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp, PDB code: 1svk was solved by C.J.Thomas, X.Du, P.Li, Y.Wang, E.M.Ross, S.R.Sprang, 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 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 79.473, 79.473, 105.209, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 23.9

Other elements in 1svk:

The structure of Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp (pdb code 1svk). 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 the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp, PDB code: 1svk:

Magnesium binding site 1 out of 1 in 1svk

Go back to Magnesium Binding Sites List in 1svk
Magnesium binding site 1 out of 1 in the Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the K180P Mutant of Gi Alpha Subunit Bound to ALF4 and Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg356

b:15.7
occ:1.00
 OG1 A:THR181 2.0 19.2 1.0
O2B A:GDP355 2.0 15.4 1.0
F3 A:ALF357 2.0 19.1 1.0
OG A:SER47 2.0 14.5 0.8
O A:HOH358 2.1 15.9 1.0
O A:HOH359 2.2 17.5 1.0
CB A:THR181 3.0 14.7 1.0
CB A:SER47 3.1 17.7 0.2
CB A:SER47 3.1 15.7 0.8
PB A:GDP355 3.2 15.8 1.0
O3B A:GDP355 3.4 15.7 1.0
F2 A:ALF357 3.5 22.1 1.0
AL A:ALF357 3.5 18.0 1.0
N A:SER47 3.8 17.3 0.2
N A:SER47 3.8 16.9 0.8
CG2 A:THR181 4.0 19.2 1.0
CA A:SER47 4.0 16.7 0.2
O A:HOH584 4.0 42.1 1.0
CA A:SER47 4.0 16.1 0.8
N A:THR181 4.0 17.3 1.0
OD2 A:ASP200 4.1 24.6 1.0
CA A:THR181 4.1 17.5 1.0
OG A:SER47 4.1 16.6 0.2
O2A A:GDP355 4.2 21.3 1.0
O1B A:GDP355 4.2 15.6 1.0
F4 A:ALF357 4.3 16.5 1.0
O3A A:GDP355 4.3 19.1 1.0
O A:VAL201 4.3 16.9 1.0
PA A:GDP355 4.5 20.3 1.0
O A:HOH736 4.6 17.1 1.0
O A:VAL179 4.6 21.2 1.0
O A:HOH552 4.7 42.3 1.0
O A:HOH505 4.7 32.8 1.0
CB A:LYS46 4.7 13.6 1.0
O1A A:GDP355 4.8 26.5 1.0
CE A:LYS46 4.8 11.7 1.0
C A:LYS46 4.9 17.7 1.0
NH1 A:ARG178 4.9 14.1 1.0

Reference:

C.J.Thomas, X.Du, P.Li, Y.Wang, E.M.Ross, S.R.Sprang. Uncoupling Conformational Change From Gtp Hydrolysis in A Heterotrimeric G Protein {Alpha}-Subunit. Proc.Natl.Acad.Sci.Usa V. 101 7560 2004.
ISSN: ISSN 0027-8424
PubMed: 15128951
DOI: 10.1073/PNAS.0304091101
Page generated: Sun Aug 10 04:44:14 2025

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