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Chlorine 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:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Small Molecule Beta-Lactone 1 Covalently Bound to K-Ras(G12S), PDB code: 7tle:

Chlorine binding site 1 out of 1 in 7tle

Go back to Chlorine Binding Sites List in 7tle
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl202

b:28.6
occ:1.00
 CL1 A:I6T202 0.0 28.6 1.0
C35 A:I6T202 1.8 27.8 1.0
C34 A:I6T202 2.6 25.6 1.0
C31 A:I6T202 2.8 21.6 1.0
N9 A:I6T202 3.0 20.1 1.0
C10 A:I6T202 3.2 20.8 1.0
C26 A:I6T202 3.3 22.9 1.0
CD1 A:TYR96 3.5 20.1 1.0
O A:HOH342 3.6 18.1 1.0
C2 A:I6T202 3.7 22.0 1.0
CE1 A:TYR96 3.7 20.1 1.0
CE A:MET72 3.8 33.4 1.0
C33 A:I6T202 3.8 23.1 1.0
O A:HOH366 4.0 37.9 1.0
CG1 A:VAL9 4.0 17.9 1.0
C7 A:I6T202 4.0 25.7 1.0
C1 A:I6T202 4.1 21.7 1.0
CB A:VAL9 4.1 20.2 1.0
C30 A:I6T202 4.1 20.1 1.0
C8 A:I6T202 4.2 28.0 1.0
C32 A:I6T202 4.5 23.9 1.0
N3 A:I6T202 4.6 23.0 1.0
C27 A:I6T202 4.7 24.8 1.0
CG A:TYR96 4.7 18.6 1.0
CG2 A:VAL9 4.9 14.8 1.0
SD A:MET72 5.0 32.5 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: Tue Jul 30 04:40:13 2024

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