Magnesium in PDB 6mta: Kras Mutant Structure in Complex with Gtp Analogue

The structure of Kras Mutant Structure in Complex with Gtp Analogue, PDB code: 6mta was solved by A.K.Bera, K.D.Westover, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.08 / 2.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.320, 83.572, 84.841, 90.00, 109.89, 90.00
R / Rfree (%)	20.4 / 24.3

The binding sites of Magnesium atom in the Kras Mutant Structure in Complex with Gtp Analogue (pdb code 6mta). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Kras Mutant Structure in Complex with Gtp Analogue, PDB code: 6mta:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Kras Mutant Structure in Complex with Gtp Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Kras Mutant Structure in Complex with Gtp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:21.3 occ:1.00 O A:HOH324 2.0 18.4 1.0 O1B A:GNP201 2.0 15.7 1.0 O A:HOH310 2.1 16.3 1.0 O1G A:GNP201 2.1 19.0 1.0 OG A:SER17 2.3 16.7 1.0 OG1 A:THR35 2.3 43.0 1.0 CB A:THR35 2.9 43.2 1.0 PG A:GNP201 3.1 20.8 1.0 PB A:GNP201 3.2 17.1 1.0 N3B A:GNP201 3.2 15.4 1.0 CB A:SER17 3.4 17.4 1.0 OD2 A:ASP57 3.8 36.1 1.0 CG2 A:THR35 3.9 40.4 1.0 O3G A:GNP201 4.0 18.8 1.0 N A:SER17 4.0 16.1 1.0 N A:THR35 4.1 50.4 1.0 O2B A:GNP201 4.1 15.6 1.0 CA A:THR35 4.1 48.4 1.0 O2A A:GNP201 4.2 19.4 1.0 OD1 A:ASP57 4.2 35.7 1.0 O3A A:GNP201 4.3 16.4 1.0 CA A:SER17 4.3 16.6 1.0 O2G A:GNP201 4.4 18.8 1.0 CG A:ASP57 4.4 35.0 1.0 O A:ASP33 4.5 49.1 1.0 O A:THR58 4.5 38.0 1.0 PA A:GNP201 4.6 16.8 1.0 O1A A:GNP201 4.8 18.4 1.0 O A:HOH312 4.9 35.8 1.0 CE A:LYS16 5.0 18.6 1.0 CB A:LYS16 5.0 15.4 1.0

Magnesium binding site 2 out of 3 in the Kras Mutant Structure in Complex with Gtp Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Kras Mutant Structure in Complex with Gtp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg202 b:26.2 occ:1.00 OG B:SER17 2.0 24.6 1.0 O B:HOH314 2.0 25.3 1.0 O2B B:GNP201 2.1 24.3 1.0 OG1 B:THR35 2.2 46.0 1.0 O B:HOH308 2.3 30.2 1.0 O3G B:GNP201 2.3 29.2 1.0 CB B:SER17 2.8 23.7 1.0 CB B:THR35 2.9 45.2 1.0 PB B:GNP201 3.4 24.3 1.0 PG B:GNP201 3.5 27.1 1.0 N3B B:GNP201 3.6 27.7 1.0 N B:SER17 3.6 21.4 1.0 CA B:SER17 3.8 21.8 1.0 N B:THR35 3.9 49.8 1.0 CG2 B:THR35 3.9 43.3 1.0 OD2 B:ASP57 3.9 34.0 1.0 CA B:THR35 4.0 47.1 1.0 O2A B:GNP201 4.2 27.8 1.0 O B:ASP33 4.3 61.8 1.0 OD1 B:ASP57 4.3 34.9 1.0 O3A B:GNP201 4.4 27.1 1.0 O1B B:GNP201 4.4 25.8 1.0 O1G B:GNP201 4.4 26.5 1.0 CG B:ASP57 4.5 34.6 1.0 O1A B:GNP201 4.6 29.5 1.0 PA B:GNP201 4.6 28.0 1.0 O2G B:GNP201 4.6 27.2 1.0 O B:THR58 4.6 29.3 1.0 C B:LYS16 4.7 20.2 1.0 CB B:LYS16 4.9 17.8 1.0 C B:ARG34 5.0 54.8 1.0

Magnesium binding site 3 out of 3 in the Kras Mutant Structure in Complex with Gtp Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Kras Mutant Structure in Complex with Gtp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg202 b:30.2 occ:1.00 OG C:SER17 2.3 26.6 1.0 O C:HOH301 2.3 30.2 1.0 O2B C:GNP201 2.4 26.9 1.0 O C:HOH328 2.5 35.4 1.0 O2G C:GNP201 2.5 37.8 1.0 OD1 C:ASP57 3.2 45.9 1.0 OD2 C:ASP57 3.2 46.3 1.0 PG C:GNP201 3.4 38.1 1.0 O C:THR58 3.5 56.9 1.0 CG C:ASP57 3.5 45.4 1.0 O3G C:GNP201 3.5 39.3 1.0 CB C:SER17 3.6 25.3 1.0 PB C:GNP201 3.7 27.3 1.0 N C:SER17 3.8 24.0 1.0 N3B C:GNP201 3.9 34.7 1.0 CA C:SER17 4.2 24.0 1.0 CE C:LYS16 4.3 20.5 1.0 CB C:LYS16 4.3 18.9 1.0 O1B C:GNP201 4.3 25.9 1.0 NZ C:LYS16 4.6 20.6 1.0 C C:THR58 4.6 55.8 1.0 C C:LYS16 4.7 23.4 1.0 O3A C:GNP201 4.9 27.8 1.0 O1G C:GNP201 4.9 40.6 1.0 CB C:ASP57 4.9 44.7 1.0 O C:ASP57 4.9 52.1 1.0

A.K.Bera, K.D.Westover. Kras Mutant Structure in Complex with Gtp Analogue To Be Published.