Magnesium in PDB 1iaq: C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate

The structure of C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate, PDB code: 1iaq was solved by M.Spoerner, C.Herrmann, I.R.Vetter, H.R.Kalbitzer, A.Wittinghofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.890, 79.060, 94.040, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 28.2

The binding sites of Magnesium atom in the C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate (pdb code 1iaq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate, PDB code: 1iaq:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg168 b:30.9 occ:1.00 OG A:SER17 2.3 41.1 1.0 O2G A:GNP167 2.5 43.6 1.0 O2B A:GNP167 2.7 41.8 1.0 OD1 A:ASP57 3.2 34.4 1.0 CB A:SER17 3.3 40.6 1.0 PG A:GNP167 3.9 42.1 1.0 PB A:GNP167 3.9 41.2 1.0 CG A:ASP57 4.0 34.7 1.0 OD2 A:ASP57 4.0 36.4 1.0 N A:SER17 4.1 47.0 1.0 O A:THR58 4.2 69.5 1.0 CA A:SER17 4.3 48.0 1.0 N3B A:GNP167 4.4 40.6 1.0 NZ A:LYS16 4.4 60.8 1.0 O1B A:GNP167 4.6 40.8 1.0 O1G A:GNP167 4.7 41.7 1.0 O3G A:GNP167 4.8 42.5 1.0 CB A:LYS16 5.0 60.4 1.0

Magnesium binding site 2 out of 3 in the C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1168 b:30.9 occ:1.00 OG B:SER17 2.4 46.6 1.0 O2G B:GNP1167 2.4 43.6 1.0 O2B B:GNP1167 2.6 41.8 1.0 OD1 B:ASP57 3.3 74.3 1.0 CB B:SER17 3.4 46.0 1.0 PG B:GNP1167 3.8 42.1 1.0 PB B:GNP1167 3.9 41.2 1.0 O B:THR58 4.0 44.4 1.0 CG B:ASP57 4.1 74.6 1.0 OD2 B:ASP57 4.1 76.3 1.0 N B:SER17 4.2 84.2 1.0 N3B B:GNP1167 4.3 40.6 1.0 CA B:SER17 4.3 85.2 1.0 NZ B:LYS16 4.4 93.5 1.0 O1B B:GNP1167 4.6 40.8 1.0 O1G B:GNP1167 4.6 41.7 1.0 O3G B:GNP1167 4.7 42.5 1.0

Magnesium binding site 3 out of 3 in the C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of C-H-Ras P21 Protein Mutant with Thr 35 Replaced By Ser (T35S) Complexed with Guanosine-5'-[B,G-Imido] Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg2168 b:30.9 occ:1.00 OG C:SER17 2.4 41.7 1.0 O2G C:GNP2167 2.4 43.6 1.0 O2B C:GNP2167 2.6 41.8 1.0 OD1 C:ASP57 3.3 62.9 1.0 CB C:SER17 3.4 41.1 1.0 PG C:GNP2167 3.8 42.1 1.0 PB C:GNP2167 3.9 41.2 1.0 CG C:ASP57 4.0 63.2 1.0 O C:THR58 4.0 46.5 1.0 OD2 C:ASP57 4.1 64.9 1.0 N C:SER17 4.2 60.1 1.0 N3B C:GNP2167 4.3 40.6 1.0 CA C:SER17 4.3 61.2 1.0 NZ C:LYS16 4.4 36.9 1.0 O1B C:GNP2167 4.6 40.8 1.0 O1G C:GNP2167 4.6 41.7 1.0 O3G C:GNP2167 4.7 42.5 1.0 CB C:LYS16 5.0 36.5 1.0

M.Spoerner, C.Herrmann, I.R.Vetter, H.R.Kalbitzer, A.Wittinghofer. Dynamic Properties of the Ras Switch I Region and Its Importance For Binding to Effectors. Proc.Natl.Acad.Sci.Usa V. 98 4944 2001.
ISSN: ISSN 0027-8424
PubMed: 11320243
DOI: 10.1073/PNAS.081441398