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Magnesium in PDB 1gia: Structure of Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis

Protein crystallography data

The structure of Structure of Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis, PDB code: 1gia was solved by A.M.Berghuis, D.E.Coleman, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.600, 80.600, 106.500, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis (pdb code 1gia). 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 Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis, PDB code: 1gia:

Magnesium binding site 1 out of 1 in 1gia

Go back to Magnesium Binding Sites List in 1gia
Magnesium binding site 1 out of 1 in the Structure of Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Active Conformations of GIA1 and the Mechanism of Gtp Hydrolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg356

b:10.8
occ:1.00
OG A:SER47 1.9 10.7 1.0
O2G A:GSP355 2.0 10.6 1.0
O A:HOH410 2.0 6.0 1.0
OG1 A:THR181 2.1 13.6 1.0
O A:HOH413 2.1 8.8 1.0
O2B A:GSP355 2.1 7.7 1.0
CB A:SER47 3.1 8.9 1.0
CB A:THR181 3.1 16.3 1.0
PG A:GSP355 3.3 16.5 1.0
PB A:GSP355 3.3 7.1 1.0
O3B A:GSP355 3.6 10.1 1.0
N A:SER47 3.9 8.1 1.0
N A:THR181 4.0 16.8 1.0
O3G A:GSP355 4.0 15.0 1.0
CA A:SER47 4.1 9.0 1.0
OD2 A:ASP200 4.1 11.8 1.0
O A:HOH462 4.1 25.2 1.0
CA A:THR181 4.1 16.1 1.0
CG2 A:THR181 4.2 13.2 1.0
OD1 A:ASP200 4.2 11.8 1.0
O2A A:GSP355 4.3 10.8 1.0
O1B A:GSP355 4.4 9.6 1.0
O3A A:GSP355 4.4 5.8 1.0
O A:VAL179 4.4 12.3 1.0
O A:VAL201 4.5 24.4 1.0
CG A:ASP200 4.6 11.9 1.0
O A:HOH432 4.6 30.0 1.0
PA A:GSP355 4.7 9.6 1.0
O1A A:GSP355 4.8 9.5 1.0
CE A:LYS46 4.9 8.8 1.0
S1G A:GSP355 4.9 15.4 1.0
CB A:LYS46 5.0 9.7 1.0

Reference:

D.E.Coleman, A.M.Berghuis, E.Lee, M.E.Linder, A.G.Gilman, S.R.Sprang. Structures of Active Conformations of Gi Alpha 1 and the Mechanism of Gtp Hydrolysis. Science V. 265 1405 1994.
ISSN: ISSN 0036-8075
PubMed: 8073283
Page generated: Mon Dec 14 05:57:47 2020

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