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Chlorine in PDB 4ls6: Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis

Enzymatic activity of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis

All present enzymatic activity of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis:
2.3.1.179;

Protein crystallography data

The structure of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis, PDB code: 4ls6 was solved by F.Trajtenberg, N.Larrieux, A.Buschiazzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.84 / 1.56
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.069, 87.974, 145.054, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 17.2

Other elements in 4ls6:

The structure of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis also contains other interesting chemical elements:

Potassium (K) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis (pdb code 4ls6). 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 Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis, PDB code: 4ls6:

Chlorine binding site 1 out of 1 in 4ls6

Go back to Chlorine Binding Sites List in 4ls6
Chlorine binding site 1 out of 1 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis


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 Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:21.6
occ:1.00
 O B:LYS206 2.6 22.4 1.0
O B:ASP226 2.7 20.0 1.0
O B:LEU208 3.0 20.7 1.0
O B:HOH872 3.0 35.6 1.0
O B:HOH673 3.1 24.0 1.0
O B:HOH646 3.1 21.6 1.0
O B:HOH861 3.3 39.3 1.0
C B:LYS206 3.7 22.0 1.0
C B:ASP226 3.8 20.6 1.0
C B:LEU208 3.8 20.4 1.0
O B:ALA207 4.1 20.4 1.0
CA B:GLY227 4.1 17.5 1.0
C B:ALA207 4.1 21.4 1.0
N B:GLY227 4.4 19.3 1.0
CA B:LYS206 4.4 18.9 1.0
CB B:LYS206 4.4 21.7 1.0
N B:LEU208 4.4 19.4 1.0
N B:SER209 4.5 17.4 1.0
CA B:SER209 4.5 18.1 1.0
N B:ALA207 4.6 18.2 1.0
CA B:ALA207 4.6 18.4 1.0
CA B:LEU208 4.7 20.3 1.0
CA B:ASP226 4.9 19.6 1.0
O B:HOH707 4.9 28.8 1.0

Reference:

F.Trajtenberg, S.Altabe, N.Larrieux, F.Ficarra, D.De Mendoza, A.Buschiazzo, G.E.Schujman. Structural Insights Into Bacterial Resistance to Cerulenin. Febs J. V. 281 2324 2014.
ISSN: ISSN 1742-464X
PubMed: 24641521
DOI: 10.1111/FEBS.12785
Page generated: Sun Jul 21 19:13:41 2024

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