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Potassium 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:

Chlorine (Cl) 1 atom

Potassium Binding Sites:

The binding sites of Potassium 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 Potassium atom.
In total 4 binding sites of Potassium where determined in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) I108F Mutant From Bacillus Subtilis, PDB code: 4ls6:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 4ls6

Go back to Potassium Binding Sites List in 4ls6
Potassium binding site 1 out of 4 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 Potassium with other atoms in the K 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
A:K501

b:16.2
occ:1.00
 OE1 A:GLU348 2.7 18.7 1.0
OD1 A:ASN300 2.7 17.9 1.0
O A:ASN394 2.7 17.1 1.0
O A:ASN300 2.8 17.1 1.0
OG A:SER393 2.9 16.9 1.0
O A:ALA301 3.0 16.4 1.0
N A:ASN394 3.5 14.7 1.0
C A:ALA301 3.5 17.6 1.0
C A:ASN300 3.5 18.4 1.0
CD A:GLU348 3.6 21.7 1.0
CB A:GLU348 3.7 15.8 1.0
C A:ASN394 3.7 16.5 1.0
CG A:ASN300 3.8 19.6 1.0
N A:HIS302 4.0 15.4 1.0
CG A:GLU348 4.0 19.1 1.0
CB A:SER393 4.0 17.3 1.0
CB A:ASN300 4.1 16.4 1.0
O A:HOH610 4.1 19.1 1.0
C A:SER393 4.1 18.7 1.0
O A:HOH605 4.1 18.6 1.0
CA A:SER393 4.2 15.3 1.0
CA A:ASN394 4.2 15.0 1.0
N A:ALA301 4.2 16.4 1.0
CA A:HIS302 4.2 15.3 1.0
CA A:ALA301 4.3 16.3 1.0
CA A:ASN300 4.4 15.8 1.0
O A:HOH618 4.6 17.8 1.0
OE2 A:GLU348 4.7 19.6 1.0
OG A:SER395 4.8 19.6 1.0
CB A:ASN394 4.9 17.5 1.0
N A:SER395 4.9 15.1 1.0
NZ A:LYS334 4.9 16.8 1.0
ND2 A:ASN300 5.0 17.7 1.0

Potassium binding site 2 out of 4 in 4ls6

Go back to Potassium Binding Sites List in 4ls6
Potassium binding site 2 out of 4 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 Potassium with other atoms in the K binding site number 2 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
A:K502

b:18.7
occ:0.70
 K A:K502 0.0 18.7 0.7
K A:K502 1.4 19.4 0.3
O A:HOH742 2.7 31.7 1.0
O A:LEU208 2.7 19.8 1.0
O A:LYS206 2.7 18.9 1.0
O A:ASP226 2.8 21.1 1.0
O A:HOH820 2.8 30.6 0.7
O A:HOH704 3.0 24.7 1.0
C A:LEU208 3.7 20.3 1.0
C A:LYS206 3.7 17.9 1.0
C A:ASP226 4.0 21.1 1.0
O A:HOH669 4.1 26.2 1.0
CA A:LYS206 4.3 15.5 1.0
CB A:LYS206 4.3 16.2 1.0
CA A:SER209 4.4 17.0 1.0
O A:HOH799 4.4 31.6 1.0
N A:SER209 4.4 17.2 1.0
C A:ALA207 4.4 17.6 1.0
O A:ALA207 4.5 18.0 1.0
N A:LEU208 4.5 15.2 1.0
OD2 A:ASP226 4.5 40.1 1.0
O A:HOH844 4.5 37.8 1.0
CA A:GLY227 4.6 16.8 1.0
O A:HOH702 4.6 29.5 1.0
CG2 A:THR210 4.6 25.1 1.0
N A:THR210 4.6 19.9 1.0
N A:ALA207 4.7 16.0 1.0
N A:GLY227 4.7 16.6 1.0
CA A:LEU208 4.8 15.7 1.0
C A:SER209 4.8 20.4 1.0
CB A:ASP226 4.9 21.5 1.0
CG A:ASP226 4.9 32.2 1.0
CA A:ASP226 4.9 18.7 1.0
CA A:ALA207 5.0 16.1 1.0

Potassium binding site 3 out of 4 in 4ls6

Go back to Potassium Binding Sites List in 4ls6
Potassium binding site 3 out of 4 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 Potassium with other atoms in the K binding site number 3 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
A:K502

b:19.4
occ:0.30
 K A:K502 0.0 19.4 0.3
K A:K502 1.4 18.7 0.7
O A:HOH820 1.9 30.6 0.7
O A:LYS206 2.5 18.9 1.0
O A:ASP226 2.7 21.1 1.0
O A:HOH669 3.1 26.2 1.0
O A:HOH702 3.5 29.5 1.0
O A:HOH742 3.6 31.7 1.0
C A:LYS206 3.7 17.9 1.0
C A:ASP226 3.7 21.1 1.0
O A:LEU208 3.8 19.8 1.0
O A:HOH651 3.9 23.5 1.0
O A:HOH704 3.9 24.7 1.0
CB A:LYS206 4.3 16.2 1.0
O A:HOH897 4.3 45.5 1.0
CA A:GLY227 4.3 16.8 1.0
O A:ALA207 4.4 18.0 1.0
N A:GLY227 4.4 16.6 1.0
CA A:LYS206 4.5 15.5 1.0
C A:ALA207 4.5 17.6 1.0
C A:LEU208 4.6 20.3 1.0
CA A:ASP226 4.6 18.7 1.0
N A:ALA207 4.7 16.0 1.0
CA A:ALA207 4.8 16.1 1.0
CB A:ASP226 4.9 21.5 1.0
N A:LEU208 5.0 15.2 1.0

Potassium binding site 4 out of 4 in 4ls6

Go back to Potassium Binding Sites List in 4ls6
Potassium binding site 4 out of 4 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 Potassium with other atoms in the K binding site number 4 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:K501

b:19.1
occ:1.00
 OE1 B:GLU348 2.7 20.2 1.0
OD1 B:ASN300 2.7 20.8 1.0
O B:ASN394 2.8 19.1 1.0
O B:ASN300 2.8 19.2 1.0
OG B:SER393 2.9 22.1 1.0
O B:ALA301 3.0 21.4 1.0
C B:ALA301 3.5 20.2 1.0
C B:ASN300 3.5 21.4 1.0
N B:ASN394 3.6 17.5 1.0
CD B:GLU348 3.6 26.0 1.0
CB B:GLU348 3.7 19.9 1.0
CG B:ASN300 3.7 21.1 1.0
C B:ASN394 3.8 20.7 1.0
CG B:GLU348 4.0 19.6 1.0
N B:HIS302 4.0 18.8 1.0
CB B:SER393 4.1 20.1 1.0
O B:HOH619 4.1 21.9 1.0
CB B:ASN300 4.1 20.4 1.0
C B:SER393 4.2 20.0 1.0
O B:HOH620 4.2 22.1 1.0
N B:ALA301 4.2 19.5 1.0
CA B:SER393 4.2 18.6 1.0
CA B:HIS302 4.2 18.2 1.0
CA B:ASN394 4.2 17.4 1.0
CA B:ALA301 4.3 18.6 1.0
CA B:ASN300 4.4 20.6 1.0
O B:HOH624 4.7 20.6 1.0
OE2 B:GLU348 4.7 22.6 1.0
OG B:SER395 4.8 21.6 1.0
NZ B:LYS334 4.9 20.9 1.0
N B:SER395 4.9 18.1 1.0
ND2 B:ASN300 4.9 20.3 1.0
CB B:ASN394 4.9 19.0 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: Mon Aug 12 11:30:32 2024

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