Potassium in PDB 6bjp: Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa

Enzymatic activity of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa

All present enzymatic activity of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa:
1.2.1.8;

Protein crystallography data

The structure of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa, PDB code: 6bjp was solved by E.I.Carrizosa-Carbajal, L.Gonzalez-Segura, R.A.Munoz-Clares, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.83 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.224, 96.543, 280.876, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 20.4

Potassium Binding Sites:

The binding sites of Potassium atom in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa (pdb code 6bjp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa, PDB code: 6bjp:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 6bjp

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Potassium binding site 1 out of 4 in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:20.8
occ:1.00
 O A:ASP93 2.7 18.8 1.0
O A:VAL180 2.7 19.4 1.0
OG1 A:THR26 2.7 23.9 1.0
OD1 A:ASP93 2.8 23.6 1.0
O A:ILE27 2.8 16.9 1.0
O A:HOH690 2.9 20.3 1.0
O A:HOH664 3.6 32.8 1.0
N A:ILE27 3.6 23.1 1.0
C A:ASP93 3.7 15.1 1.0
CG A:ASP93 3.7 23.1 1.0
C A:ILE27 3.8 20.7 1.0
C A:VAL180 3.9 23.4 1.0
CA A:ASP93 4.0 16.1 1.0
CB A:THR26 4.0 19.8 1.0
C A:THR26 4.3 23.9 1.0
CA A:ILE27 4.3 23.3 1.0
CA A:THR26 4.4 19.4 1.0
CB A:ASP93 4.4 20.1 1.0
OD2 A:ASP93 4.6 20.0 1.0
CG2 A:THR181 4.6 24.0 1.0
CA A:THR181 4.6 20.0 1.0
CD A:PRO29 4.6 15.7 1.0
O A:VAL329 4.6 17.5 1.0
CD1 A:LEU35 4.7 17.5 1.0
CG1 A:VAL180 4.7 16.4 1.0
N A:THR181 4.7 18.1 1.0
N A:ASN28 4.8 19.4 1.0
N A:THR94 4.9 14.5 1.0
CA A:VAL180 4.9 17.9 1.0
O A:HOH656 5.0 25.4 1.0

Potassium binding site 2 out of 4 in 6bjp

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Potassium binding site 2 out of 4 in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K501

b:27.0
occ:1.00
 O B:ILE27 2.6 30.7 1.0
O B:VAL180 2.7 27.4 1.0
O B:ASP93 2.8 23.1 1.0
OG1 B:THR26 2.8 32.6 1.0
O B:HOH635 2.9 25.1 1.0
OD1 B:ASP93 2.9 30.9 1.0
N B:ILE27 3.5 29.4 1.0
C B:ILE27 3.6 31.3 1.0
C B:ASP93 3.7 28.3 1.0
C B:VAL180 3.9 28.2 1.0
CG B:ASP93 3.9 32.0 1.0
CA B:ASP93 4.0 26.5 1.0
CB B:THR26 4.1 29.2 1.0
CA B:ILE27 4.2 32.8 1.0
C B:THR26 4.2 33.3 1.0
CA B:THR26 4.4 33.3 1.0
CB B:ASP93 4.5 21.6 1.0
CG2 B:THR181 4.6 21.4 1.0
CD B:PRO29 4.6 21.0 1.0
CG1 B:VAL180 4.6 31.7 1.0
CA B:THR181 4.7 21.6 1.0
CD1 B:LEU35 4.7 27.0 1.0
N B:ASN28 4.7 28.2 1.0
N B:THR181 4.8 24.5 1.0
O B:VAL329 4.8 23.2 1.0
OD2 B:ASP93 4.8 31.2 1.0
CA B:VAL180 4.9 28.7 1.0
N B:THR94 5.0 20.0 1.0
CB B:ILE27 5.0 39.3 1.0

Potassium binding site 3 out of 4 in 6bjp

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Potassium binding site 3 out of 4 in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K501

b:26.4
occ:1.00
 O C:VAL180 2.7 23.8 1.0
OG1 C:THR26 2.7 24.9 1.0
O C:ASP93 2.7 20.7 1.0
O C:ILE27 2.8 18.1 1.0
O C:HOH723 2.9 27.6 1.0
OD1 C:ASP93 2.9 16.6 1.0
O C:HOH655 3.3 38.4 1.0
N C:ILE27 3.6 21.1 1.0
C C:ASP93 3.7 21.7 1.0
C C:ILE27 3.8 24.6 1.0
CG C:ASP93 3.9 28.7 1.0
C C:VAL180 3.9 27.1 1.0
CB C:THR26 4.0 24.1 1.0
CA C:ASP93 4.0 22.8 1.0
C C:THR26 4.2 21.5 1.0
CA C:ILE27 4.3 22.1 1.0
CA C:THR26 4.3 22.8 1.0
CB C:ASP93 4.5 23.6 1.0
CA C:THR181 4.6 19.1 1.0
CD1 C:LEU35 4.7 25.7 1.0
CG1 C:VAL180 4.7 32.1 1.0
CG2 C:THR181 4.7 16.6 1.0
OD2 C:ASP93 4.7 27.4 1.0
CD C:PRO29 4.7 20.6 1.0
N C:THR181 4.7 17.8 1.0
O C:VAL329 4.7 27.9 1.0
N C:ASN28 4.8 18.7 1.0
CA C:VAL180 4.9 19.1 1.0
N C:THR94 4.9 19.6 1.0
O C:HOH621 5.0 28.6 1.0

Potassium binding site 4 out of 4 in 6bjp

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Potassium binding site 4 out of 4 in the Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Apo Form of the E124S Mutant of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K501

b:46.5
occ:1.00
 O D:VAL180 2.7 48.4 1.0
O D:ASP93 2.8 46.5 1.0
O D:ILE27 2.8 44.8 1.0
O D:HOH643 2.8 41.4 1.0
OD1 D:ASP93 2.9 43.1 1.0
OG1 D:THR26 2.9 40.9 1.0
N D:ILE27 3.6 51.3 1.0
C D:ILE27 3.7 46.0 1.0
C D:ASP93 3.8 43.2 1.0
CG D:ASP93 3.9 41.4 1.0
C D:VAL180 3.9 44.8 1.0
CA D:ASP93 4.1 42.9 1.0
CB D:THR26 4.1 47.5 1.0
CA D:ILE27 4.2 47.5 1.0
C D:THR26 4.2 53.4 1.0
CA D:THR26 4.4 51.0 1.0
CG1 D:VAL180 4.5 42.0 1.0
O D:VAL329 4.6 40.1 1.0
CB D:ASP93 4.6 39.9 1.0
CD D:PRO29 4.7 47.3 1.0
CG2 D:THR181 4.7 41.1 1.0
OD2 D:ASP93 4.7 38.8 1.0
N D:ASN28 4.7 42.2 1.0
CA D:THR181 4.8 39.1 1.0
CA D:VAL180 4.8 43.5 1.0
N D:THR181 4.8 38.6 1.0
CD1 D:LEU35 4.9 49.2 1.0
N D:THR94 5.0 43.5 1.0

Reference:

E.I.Carrizosa-Carbajal, L.Gonzalez-Segura, R.A.Munoz-Clares. Structural Role of GLU124 of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa To Be Published.
Page generated: Mon Dec 14 00:18:45 2020

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