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Potassium in PDB 4ls7: Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin

Enzymatic activity of Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin

All present enzymatic activity of Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin:
2.3.1.179;

Protein crystallography data

The structure of Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin, PDB code: 4ls7 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) 28.92 / 1.67
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.266, 87.721, 144.730, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin (pdb code 4ls7). 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 Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin, PDB code: 4ls7:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 4ls7

Go back to Potassium Binding Sites List in 4ls7
Potassium binding site 1 out of 4 in the Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin


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 Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:16.9
occ:1.00
 OE1 A:GLU348 2.6 18.9 1.0
O A:ASN394 2.7 16.7 1.0
OD1 A:ASN300 2.7 16.5 1.0
O A:ASN300 2.8 16.2 1.0
OG A:SER393 2.9 17.0 1.0
O A:ALA301 2.9 17.6 1.0
C A:ALA301 3.5 15.3 1.0
N A:ASN394 3.5 14.3 1.0
C A:ASN300 3.6 18.3 1.0
CD A:GLU348 3.6 20.8 1.0
CB A:GLU348 3.7 17.7 1.0
C A:ASN394 3.7 16.9 1.0
CG A:ASN300 3.8 18.8 1.0
O A:HOH617 3.9 19.1 1.0
N A:HIS302 3.9 15.9 1.0
CB A:SER393 4.0 18.0 1.0
CG A:GLU348 4.1 20.1 1.0
C A:SER393 4.1 17.3 1.0
O A:HOH607 4.1 18.2 1.0
CB A:ASN300 4.1 17.0 1.0
CA A:HIS302 4.2 13.5 1.0
CA A:SER393 4.2 15.1 1.0
CA A:ASN394 4.2 13.2 1.0
N A:ALA301 4.2 16.1 1.0
CA A:ALA301 4.3 15.2 1.0
CA A:ASN300 4.5 15.9 1.0
OE2 A:GLU348 4.7 18.6 1.0
OG A:SER395 4.7 22.0 1.0
O A:HOH615 4.7 18.4 1.0
N A:SER395 4.9 19.2 1.0
CB A:ASN394 4.9 19.2 1.0
NZ A:LYS334 4.9 16.8 1.0
ND2 A:ASN300 5.0 18.2 1.0

Potassium binding site 2 out of 4 in 4ls7

Go back to Potassium Binding Sites List in 4ls7
Potassium binding site 2 out of 4 in the Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin


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 Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K502

b:23.4
occ:1.00
 O A:ASP226 2.7 20.0 1.0
O A:LEU208 2.7 18.9 1.0
O A:HOH665 2.8 29.3 1.0
O A:LYS206 2.8 18.2 1.0
O A:HOH740 2.8 29.3 1.0
O A:HOH648 2.9 22.1 1.0
C A:LEU208 3.7 15.8 1.0
C A:LYS206 3.7 17.1 1.0
C A:ASP226 3.9 19.4 1.0
O A:HOH747 4.1 29.6 1.0
O A:HOH680 4.2 25.1 1.0
CA A:LYS206 4.3 13.5 1.0
CB A:LYS206 4.3 15.6 1.0
N A:SER209 4.4 15.4 1.0
CA A:SER209 4.4 18.2 1.0
N A:LEU208 4.5 16.7 1.0
C A:ALA207 4.5 16.7 1.0
OD2 A:ASP226 4.5 28.1 1.0
CA A:GLY227 4.5 16.0 1.0
CG2 A:THR210 4.5 27.2 1.0
O A:ALA207 4.6 17.4 1.0
N A:THR210 4.7 19.8 1.0
N A:GLY227 4.7 16.8 1.0
CA A:LEU208 4.7 17.2 1.0
N A:ALA207 4.7 16.1 1.0
O A:HOH703 4.7 28.0 1.0
CB A:ASP226 4.8 25.2 1.0
CG A:ASP226 4.8 28.3 1.0
CA A:ASP226 4.8 18.6 1.0
C A:SER209 4.9 20.9 1.0
O A:HOH883 4.9 41.1 1.0

Potassium binding site 3 out of 4 in 4ls7

Go back to Potassium Binding Sites List in 4ls7
Potassium binding site 3 out of 4 in the Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin


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 Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K501

b:18.9
occ:1.00
 OE1 B:GLU348 2.7 21.1 0.2
OE1 B:GLU348 2.7 21.3 0.8
OD1 B:ASN300 2.7 19.1 1.0
O B:ASN300 2.7 18.8 1.0
O B:ASN394 2.8 18.9 1.0
OG B:SER393 2.9 18.7 1.0
O B:ALA301 3.0 21.1 1.0
C B:ALA301 3.5 19.5 1.0
C B:ASN300 3.6 21.6 1.0
N B:ASN394 3.6 18.2 1.0
CD B:GLU348 3.6 20.9 0.2
CD B:GLU348 3.6 21.1 0.8
CB B:GLU348 3.7 18.2 0.8
CB B:GLU348 3.7 17.7 0.2
CG B:ASN300 3.7 18.6 1.0
C B:ASN394 3.8 22.0 1.0
N B:HIS302 4.0 18.9 1.0
O B:HOH632 4.1 19.5 1.0
CB B:SER393 4.1 19.5 1.0
CG B:GLU348 4.1 17.7 0.8
CG B:GLU348 4.1 18.9 0.2
CB B:ASN300 4.1 22.2 1.0
O B:HOH605 4.1 19.5 1.0
CA B:HIS302 4.2 15.8 1.0
C B:SER393 4.2 16.8 1.0
CA B:SER393 4.2 18.3 1.0
CA B:ASN394 4.2 18.5 1.0
N B:ALA301 4.2 20.6 1.0
CA B:ALA301 4.4 19.6 1.0
CA B:ASN300 4.5 18.8 1.0
OE2 B:GLU348 4.6 22.2 0.2
O B:HOH624 4.6 20.5 1.0
OE2 B:GLU348 4.7 23.4 0.8
OG B:SER395 4.7 21.6 1.0
NZ B:LYS334 4.9 19.9 1.0
CB B:ASN394 4.9 19.2 1.0
ND2 B:ASN300 4.9 20.2 1.0
N B:SER395 5.0 21.0 1.0

Potassium binding site 4 out of 4 in 4ls7

Go back to Potassium Binding Sites List in 4ls7
Potassium binding site 4 out of 4 in the Crystal Structure of Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin


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 Bacillus Subtilis Beta-Ketoacyl-Acp Synthase II (Fabf) in A Non-Covalent Complex with Cerulenin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K502

b:24.4
occ:1.00
 O B:LYS206 2.6 25.5 1.0
O B:ASP226 2.7 20.6 1.0
O B:LEU208 2.8 21.6 1.0
O B:HOH658 3.0 27.1 1.0
O B:HOH660 3.5 24.4 1.0
C B:LYS206 3.6 26.2 1.0
C B:LEU208 3.7 21.0 1.0
C B:ASP226 3.8 20.1 1.0
C B:ALA207 4.2 22.1 1.0
CA B:GLY227 4.2 16.1 1.0
O B:ALA207 4.2 22.0 1.0
CA B:LYS206 4.3 18.3 1.0
N B:LEU208 4.3 21.6 1.0
N B:SER209 4.4 17.8 1.0
CB B:LYS206 4.4 24.3 1.0
CA B:SER209 4.4 20.0 1.0
O B:HOH798 4.4 42.4 1.0
N B:GLY227 4.5 19.2 1.0
N B:ALA207 4.5 22.1 1.0
CA B:LEU208 4.7 23.3 1.0
CA B:ALA207 4.7 19.3 1.0
CA B:ASP226 4.9 22.0 1.0
O B:HOH671 4.9 25.6 1.0
N B:THR210 5.0 19.7 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 11:31:52 2024

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