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Magnesium in PDB 4n0d: Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas

Enzymatic activity of Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas

All present enzymatic activity of Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas:
3.6.5.1;

Protein crystallography data

The structure of Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas, PDB code: 4n0d was solved by T.M.Thaker, A.M.Preininger, M.Sarwar, H.E.Hamm, T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.81 / 1.55
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 79.635, 79.635, 104.825, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas (pdb code 4n0d). 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 the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas, PDB code: 4n0d:

Magnesium binding site 1 out of 1 in 4n0d

Go back to Magnesium Binding Sites List in 4n0d
Magnesium binding site 1 out of 1 in the Crystal Structure of the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas


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 the K345L Variant of the Gi ALPHA1 Subunit Bound to Gtpgammas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:16.1
occ:1.00
O A:HOH634 2.0 18.0 1.0
OG A:SER47 2.0 15.6 1.0
O2B A:GSP403 2.1 15.1 1.0
O A:HOH633 2.1 17.1 1.0
O2G A:GSP403 2.1 15.5 1.0
OG1 A:THR181 2.1 17.8 1.0
CB A:SER47 3.1 15.2 1.0
CB A:THR181 3.1 17.4 1.0
PB A:GSP403 3.2 15.9 1.0
PG A:GSP403 3.3 15.6 1.0
O3B A:GSP403 3.4 15.7 1.0
N A:SER47 3.9 14.8 1.0
OD2 A:ASP200 3.9 20.3 1.0
N A:THR181 4.0 16.4 1.0
O3G A:GSP403 4.0 18.6 1.0
CA A:SER47 4.1 15.1 1.0
OD1 A:ASP200 4.1 20.9 1.0
CG2 A:THR181 4.1 18.3 1.0
CA A:THR181 4.1 17.6 1.0
O A:HOH635 4.2 27.1 1.0
O2A A:GSP403 4.2 18.0 1.0
O1B A:GSP403 4.2 15.9 1.0
O3A A:GSP403 4.3 14.0 1.0
CG A:ASP200 4.4 19.9 1.0
O A:VAL179 4.5 20.4 1.0
PA A:GSP403 4.6 16.6 1.0
O A:VAL201 4.6 19.3 1.0
O1A A:GSP403 4.8 16.5 1.0
CB A:LYS46 4.8 15.5 1.0
O A:HOH711 4.9 33.5 1.0
O A:HOH536 4.9 20.4 1.0
CE A:LYS46 4.9 15.7 1.0
S1G A:GSP403 4.9 18.0 1.0
C A:LYS46 5.0 15.3 1.0

Reference:

T.M.Thaker, M.Sarwar, A.M.Preininger, H.E.Hamm, T.M.Iverson. A Transient Interaction Between the Phosphate Binding Loop and Switch I Contributes to the Allosteric Network Between Receptor and Nucleotide in G Alpha I1. J.Biol.Chem. V. 289 11331 2014.
ISSN: ISSN 0021-9258
PubMed: 24596087
DOI: 10.1074/JBC.M113.539064
Page generated: Mon Aug 19 23:23:20 2024

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