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Magnesium in PDB 7tle: Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S)

Enzymatic activity of Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S)

All present enzymatic activity of Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S):
3.6.5.2;

Protein crystallography data

The structure of Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S), PDB code: 7tle was solved by Z.Ziyang, K.Z.Guiley, K.M.Shokat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.65 / 1.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.78, 50.66, 89.31, 90, 90, 90
R / Rfree (%) 18.9 / 23.4

Other elements in 7tle:

The structure of Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S) (pdb code 7tle). 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 Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S), PDB code: 7tle:

Magnesium binding site 1 out of 1 in 7tle

Go back to Magnesium Binding Sites List in 7tle
Magnesium binding site 1 out of 1 in the Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S)


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 Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:17.6
occ:1.00
 O A:HOH317 2.0 22.3 1.0
O A:HOH339 2.1 24.3 1.0
O A:HOH309 2.1 21.3 1.0
O2B A:GDP203 2.1 19.2 1.0
O A:HOH349 2.2 23.8 1.0
OG A:SER17 2.3 21.4 1.0
PB A:GDP203 3.3 21.3 1.0
CB A:SER17 3.4 20.2 1.0
O1B A:GDP203 3.4 20.2 1.0
N A:SER17 4.0 18.2 1.0
O1A A:GDP203 4.1 26.0 1.0
CB A:ALA59 4.2 23.9 1.0
OD2 A:ASP57 4.2 22.2 1.0
CD1 A:TYR32 4.2 31.7 1.0
CA A:SER17 4.3 18.1 1.0
OD1 A:ASP57 4.3 21.8 1.0
O3B A:GDP203 4.3 19.3 1.0
O3A A:GDP203 4.4 22.1 1.0
O A:THR58 4.5 20.7 1.0
CE1 A:TYR32 4.5 29.1 1.0
PA A:GDP203 4.6 23.4 1.0
CA A:PRO34 4.6 34.6 1.0
CG A:ASP57 4.6 21.1 1.0
O2A A:GDP203 4.6 23.0 1.0
O A:ASP33 4.7 34.8 1.0
O A:PRO34 4.7 34.6 1.0
O A:ILE36 4.7 23.2 1.0
O A:HOH303 4.9 32.3 1.0
NZ A:LYS16 4.9 21.3 1.0
O A:HOH340 4.9 26.6 1.0
CB A:LYS16 4.9 15.0 1.0

Reference:

Z.Zhang, K.Z.Guiley, K.M.Shokat. Chemical Acylation of An Acquired Serine Suppresses Oncogenic Signaling of K-Ras(G12S). Nat.Chem.Biol. V. 18 1177 2022.
ISSN: ESSN 1552-4469
PubMed: 35864332
DOI: 10.1038/S41589-022-01065-9
Page generated: Thu Oct 3 09:20:28 2024

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