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Magnesium in PDB 1svs: Structure of the K180P Mutant of Gi Alpha Subunit Bound to Gppnhp.

Enzymatic activity of Structure of the K180P Mutant of Gi Alpha Subunit Bound to Gppnhp.

All present enzymatic activity of Structure of the K180P Mutant of Gi Alpha Subunit Bound to Gppnhp.:
3.6.1.46;

Protein crystallography data

The structure of Structure of the K180P Mutant of Gi Alpha Subunit Bound to Gppnhp., PDB code: 1svs 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 / 1.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 79.317, 79.317, 105.141, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 20.9

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 1svs

Go back to Magnesium Binding Sites List in 1svs
Magnesium binding site 1 out of 1 in the Structure of the K180P Mutant of Gi Alpha Subunit Bound to Gppnhp.


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 Gppnhp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg356

b:10.7
occ:1.00
OG A:SER47 2.1 12.0 1.0
O1B A:GNP355 2.1 12.5 1.0
O2G A:GNP355 2.2 12.4 1.0
OG1 A:THR181 2.2 13.1 1.0
O A:HOH581 2.2 12.8 1.0
O A:HOH401 2.2 11.7 1.0
CB A:THR181 3.1 13.7 1.0
CB A:SER47 3.2 10.8 1.0
PB A:GNP355 3.2 9.9 1.0
PG A:GNP355 3.3 10.6 1.0
N3B A:GNP355 3.4 11.1 1.0
N A:THR181 3.7 13.1 1.0
N A:SER47 3.9 10.2 1.0
OD2 A:ASP200 3.9 17.2 1.0
CA A:THR181 4.0 14.3 1.0
O3G A:GNP355 4.0 11.7 1.0
CA A:SER47 4.1 9.3 1.0
O2A A:GNP355 4.2 12.3 1.0
O A:HOH446 4.2 23.1 1.0
OD1 A:ASP200 4.3 17.3 1.0
CG2 A:THR181 4.3 14.7 1.0
O3A A:GNP355 4.3 10.3 1.0
O2B A:GNP355 4.3 11.6 1.0
O1G A:GNP355 4.4 13.3 1.0
CG A:ASP200 4.5 16.7 1.0
O A:VAL179 4.5 14.7 1.0
O A:VAL201 4.5 15.1 1.0
PA A:GNP355 4.6 10.3 1.0
C A:PRO180 4.7 14.1 1.0
O1A A:GNP355 4.7 11.2 1.0
CB A:LYS46 4.8 10.3 1.0
CE A:LYS46 4.8 12.0 1.0
O A:HOH442 4.9 14.6 1.0
CA A:PRO180 4.9 13.5 1.0
C A:LYS46 4.9 10.0 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: Tue Aug 13 14:20:03 2024

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