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Magnesium in PDB 6ase: Kras Mutant-A59G in Gdp-Bound

Protein crystallography data

The structure of Kras Mutant-A59G in Gdp-Bound, PDB code: 6ase was solved by K.Westover, J.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.59 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.434, 47.428, 89.703, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Kras Mutant-A59G in Gdp-Bound (pdb code 6ase). 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 Kras Mutant-A59G in Gdp-Bound, PDB code: 6ase:

Magnesium binding site 1 out of 1 in 6ase

Go back to Magnesium Binding Sites List in 6ase
Magnesium binding site 1 out of 1 in the Kras Mutant-A59G in Gdp-Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Kras Mutant-A59G in Gdp-Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:22.5
occ:1.00
OG A:SER17 2.0 23.1 1.0
O A:HOH323 2.0 20.5 1.0
O1B A:GDP202 2.1 20.6 1.0
O A:HOH310 2.1 26.0 1.0
O A:HOH339 2.1 26.1 1.0
O A:HOH362 2.1 28.6 1.0
CB A:SER17 3.2 23.5 1.0
PB A:GDP202 3.2 22.7 1.0
O3B A:GDP202 3.4 26.0 1.0
N A:SER17 3.9 22.1 1.0
OD2 A:ASP57 4.0 26.0 1.0
O2A A:GDP202 4.1 22.2 1.0
CA A:SER17 4.1 25.1 1.0
OD1 A:ASP57 4.1 22.1 1.0
O A:HOH368 4.2 36.9 1.0
O A:PRO34 4.2 45.2 1.0
O2B A:GDP202 4.3 21.1 1.0
O3A A:GDP202 4.3 23.8 1.0
O A:HOH345 4.4 27.1 1.0
CG A:ASP57 4.5 22.7 1.0
PA A:GDP202 4.6 26.1 1.0
O1A A:GDP202 4.7 25.1 1.0
O A:THR58 4.8 27.1 1.0
NZ A:LYS16 4.9 19.9 0.5
CB A:LYS16 4.9 18.8 0.5
O A:HOH346 4.9 35.8 1.0
CB A:LYS16 4.9 18.8 0.5
C A:LYS16 5.0 22.2 0.5
C A:LYS16 5.0 22.2 0.5
CE A:LYS16 5.0 24.3 0.5

Reference:

J.Lu, A.K.Bera, S.Gondi, K.D.Westover. Kras Switch Mutants D33E and A59G Crystallize in the State 1 Conformation. Biochemistry V. 57 324 2018.
ISSN: ISSN 1520-4995
PubMed: 29235861
DOI: 10.1021/ACS.BIOCHEM.7B00974
Page generated: Mon Sep 30 19:20:20 2024

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