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Potassium in PDB 4ls5: Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis

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

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

Protein crystallography data

The structure of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis, PDB code: 4ls5 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) 28.98 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.513, 87.522, 144.630, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19.5

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis (pdb code 4ls5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis, PDB code: 4ls5:
Jump to Potassium binding site number: 1; 2; 3; 4; 5;

Potassium binding site 1 out of 5 in 4ls5

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Potassium binding site 1 out of 5 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) 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) From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:18.4
occ:1.00
 OE1 A:GLU348 2.6 23.1 1.0
OD1 A:ASN300 2.7 17.9 1.0
O A:ASN394 2.7 16.4 1.0
O A:ASN300 2.7 20.3 1.0
OG A:SER393 3.0 22.7 1.0
O A:ALA301 3.0 18.8 1.0
C A:ALA301 3.5 21.2 1.0
C A:ASN300 3.6 21.6 1.0
N A:ASN394 3.6 15.6 1.0
CD A:GLU348 3.6 21.4 1.0
CG A:ASN300 3.7 20.2 1.0
CB A:GLU348 3.7 18.1 1.0
C A:ASN394 3.7 17.0 1.0
N A:HIS302 4.0 17.7 1.0
O A:HOH633 4.0 25.5 1.0
CG A:GLU348 4.0 17.8 1.0
CB A:SER393 4.1 18.5 1.0
CB A:ASN300 4.1 19.3 1.0
C A:SER393 4.1 21.4 1.0
O A:HOH625 4.2 21.5 1.0
CA A:SER393 4.2 16.8 1.0
CA A:ASN394 4.2 16.2 1.0
CA A:HIS302 4.2 19.3 1.0
N A:ALA301 4.2 18.4 1.0
CA A:ALA301 4.3 20.1 1.0
CA A:ASN300 4.5 18.8 1.0
OE2 A:GLU348 4.6 23.8 1.0
O A:HOH602 4.7 18.5 1.0
OG A:SER395 4.8 21.4 1.0
N A:SER395 4.9 18.6 1.0
CB A:ASN394 4.9 21.9 1.0
NZ A:LYS334 4.9 18.9 1.0
ND2 A:ASN300 4.9 24.1 1.0

Potassium binding site 2 out of 5 in 4ls5

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Potassium binding site 2 out of 5 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) 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) From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K502

b:28.5
occ:0.69
 K A:K502 0.0 28.5 0.7
K A:K502 0.4 21.7 0.3
O A:LEU208 2.7 21.2 1.0
O A:ASP226 2.7 22.6 1.0
O A:HOH799 2.8 37.1 1.0
O A:LYS206 2.8 19.4 1.0
O A:HOH729 2.9 25.9 1.0
C A:LEU208 3.6 20.2 1.0
C A:LYS206 3.7 20.9 1.0
C A:ASP226 3.9 26.9 1.0
O A:HOH674 4.0 23.6 1.0
CA A:SER209 4.2 24.6 1.0
N A:SER209 4.3 18.8 1.0
CA A:LYS206 4.3 16.2 1.0
CB A:LYS206 4.3 17.2 1.0
O A:HOH793 4.4 34.8 1.0
C A:ALA207 4.4 18.1 1.0
N A:LEU208 4.5 18.1 1.0
O A:ALA207 4.5 18.4 1.0
CA A:GLY227 4.5 18.8 1.0
N A:THR210 4.5 21.8 1.0
CA A:LEU208 4.7 19.0 1.0
CG2 A:THR210 4.7 25.1 1.0
N A:GLY227 4.7 19.1 1.0
O A:HOH916 4.7 48.5 1.0
C A:SER209 4.7 23.3 1.0
OD2 A:ASP226 4.7 45.5 1.0
N A:ALA207 4.7 15.2 1.0
CB A:ASP226 4.9 27.3 1.0
O A:HOH669 4.9 27.8 1.0
CG A:ASP226 4.9 37.2 1.0
CA A:ASP226 5.0 24.9 1.0
CA A:ALA207 5.0 18.7 1.0

Potassium binding site 3 out of 5 in 4ls5

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Potassium binding site 3 out of 5 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) 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) From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K502

b:21.7
occ:0.31
 K A:K502 0.0 21.7 0.3
K A:K502 0.4 28.5 0.7
O A:ASP226 2.7 22.6 1.0
O A:LYS206 2.8 19.4 1.0
O A:HOH799 2.8 37.1 1.0
O A:HOH729 3.0 25.9 1.0
O A:LEU208 3.1 21.2 1.0
C A:LYS206 3.8 20.9 1.0
C A:ASP226 3.9 26.9 1.0
O A:HOH674 4.0 23.6 1.0
C A:LEU208 4.0 20.2 1.0
CB A:LYS206 4.2 17.2 1.0
CA A:LYS206 4.4 16.2 1.0
CA A:SER209 4.5 24.6 1.0
O A:HOH669 4.5 27.8 1.0
CA A:GLY227 4.6 18.8 1.0
N A:SER209 4.6 18.8 1.0
C A:ALA207 4.7 18.1 1.0
O A:HOH793 4.7 34.8 1.0
O A:ALA207 4.7 18.4 1.0
O A:HOH916 4.7 48.5 1.0
N A:GLY227 4.7 19.1 1.0
CB A:ASP226 4.8 27.3 1.0
OD2 A:ASP226 4.8 45.5 1.0
N A:LEU208 4.8 18.1 1.0
N A:THR210 4.8 21.8 1.0
CA A:ASP226 4.9 24.9 1.0
N A:ALA207 4.9 15.2 1.0
O A:HOH681 4.9 26.3 1.0
CG A:ASP226 4.9 37.2 1.0
CG2 A:THR210 4.9 25.1 1.0

Potassium binding site 4 out of 5 in 4ls5

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Potassium binding site 4 out of 5 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) 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) From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K501

b:24.2
occ:1.00
 OD1 B:ASN300 2.7 28.4 1.0
O B:ASN300 2.7 22.9 1.0
OE1 B:GLU348 2.7 28.5 1.0
O B:ASN394 2.8 22.7 1.0
O B:ALA301 2.9 22.4 1.0
OG B:SER393 3.0 25.4 1.0
C B:ALA301 3.5 23.0 1.0
C B:ASN300 3.5 24.5 1.0
N B:ASN394 3.6 23.0 1.0
CD B:GLU348 3.7 26.9 1.0
CG B:ASN300 3.7 27.6 1.0
C B:ASN394 3.8 23.9 1.0
CB B:GLU348 3.8 22.2 1.0
N B:HIS302 4.0 23.2 1.0
O B:HOH668 4.0 26.1 1.0
CB B:SER393 4.1 21.8 1.0
CG B:GLU348 4.1 23.4 1.0
CB B:ASN300 4.1 27.1 1.0
CA B:HIS302 4.1 21.3 1.0
O B:HOH700 4.1 31.4 1.0
C B:SER393 4.2 26.2 1.0
CA B:ASN394 4.2 25.0 1.0
N B:ALA301 4.2 27.4 1.0
CA B:SER393 4.2 23.0 1.0
CA B:ALA301 4.3 24.0 1.0
CA B:ASN300 4.5 24.8 1.0
OE2 B:GLU348 4.7 25.9 1.0
O B:HOH650 4.7 22.9 1.0
NZ B:LYS334 4.8 24.1 1.0
OG B:SER395 4.8 22.5 1.0
CB B:ASN394 4.9 28.5 1.0
N B:SER395 4.9 24.5 1.0
ND2 B:ASN300 4.9 26.8 1.0

Potassium binding site 5 out of 5 in 4ls5

Go back to Potassium Binding Sites List in 4ls5
Potassium binding site 5 out of 5 in the Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of Beta-Ketoacyl-Acp Synthase II (Fabf) From Bacillus Subtilis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K502

b:31.6
occ:1.00
 O B:LYS206 2.7 38.0 1.0
O B:ASP226 2.7 26.7 1.0
O B:HOH778 2.7 46.4 1.0
O B:LEU208 2.8 26.8 1.0
O B:HOH646 3.0 31.0 1.0
O B:HOH693 3.3 27.7 1.0
C B:LYS206 3.7 32.7 1.0
C B:LEU208 3.8 28.0 1.0
C B:ASP226 3.9 27.0 1.0
O B:ALA207 4.2 23.1 1.0
CA B:GLY227 4.2 24.6 1.0
C B:ALA207 4.2 29.6 1.0
CA B:LYS206 4.4 25.2 1.0
CA B:SER209 4.4 25.2 1.0
N B:SER209 4.4 23.5 1.0
CB B:LYS206 4.5 28.3 1.0
N B:GLY227 4.5 28.0 1.0
N B:LEU208 4.5 26.4 1.0
N B:ALA207 4.6 24.3 1.0
CA B:ALA207 4.7 28.2 1.0
CA B:LEU208 4.8 24.1 1.0
O B:HOH801 4.9 36.9 1.0
CA B:ASP226 5.0 28.7 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 11:29:38 2024

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