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Potassium in PDB 1bw9: Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate

Enzymatic activity of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate

All present enzymatic activity of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate:
1.4.1.20;

Protein crystallography data

The structure of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate, PDB code: 1bw9 was solved by J.L.Vanhooke, J.B.Thoden, N.M.W.Brunhuber, J.L.Blanchard, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.300, 110.200, 113.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1bw9:

The structure of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate (pdb code 1bw9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate, PDB code: 1bw9:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1bw9

Go back to Potassium Binding Sites List in 1bw9
Potassium binding site 1 out of 2 in the Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K850

b:27.4
occ:1.00
O A:THR121 2.7 11.3 1.0
O A:HOH656 2.7 28.3 1.0
O B:HOH884 2.8 27.7 1.0
O A:ASP118 2.9 10.2 1.0
O A:HOH728 3.1 33.1 1.0
O A:HOH771 3.5 41.0 1.0
C A:ASP118 3.7 5.7 1.0
O A:HOH395 3.7 19.6 1.0
O A:HOH761 3.9 45.8 1.0
C A:THR121 3.9 16.2 1.0
CB A:PRO117 4.0 5.7 1.0
N A:ASP118 4.0 7.0 1.0
CA A:ASP118 4.2 8.0 1.0
C5N A:NAD360 4.3 16.0 1.0
O A:HOH689 4.4 38.3 1.0
N A:THR121 4.5 6.7 1.0
O1 B:EDO874 4.5 29.0 1.0
O1N A:NAD360 4.6 23.6 1.0
C A:PRO117 4.6 10.3 1.0
N A:VAL119 4.7 8.0 1.0
CA A:ASN122 4.7 12.9 1.0
N A:ASN122 4.8 12.1 1.0
CA A:THR121 4.8 8.8 1.0
CA A:PRO117 4.8 5.8 1.0
N A:ASN120 4.9 9.7 1.0
CA A:VAL119 4.9 8.0 1.0
C4N A:NAD360 5.0 35.3 1.0

Potassium binding site 2 out of 2 in 1bw9

Go back to Potassium Binding Sites List in 1bw9
Potassium binding site 2 out of 2 in the Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and Phenylpyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K853

b:14.6
occ:1.00
O B:HOH993 2.6 15.4 1.0
O B:SER572 2.6 9.3 1.0
O B:ASP574 2.7 10.8 1.0
O B:HOH1140 2.9 24.0 1.0
O B:LEU570 3.0 5.5 1.0
CD2 B:LEU576 3.6 5.0 1.0
C B:SER572 3.7 5.5 1.0
CG B:LEU576 3.7 11.0 1.0
C B:ASP574 3.8 11.1 1.0
N B:SER572 3.8 11.2 1.0
C B:LEU570 4.3 6.0 1.0
OG B:SER572 4.3 20.6 1.0
CA B:SER572 4.4 7.8 1.0
N B:ASP574 4.4 7.3 1.0
CD1 B:LEU576 4.5 6.7 1.0
C B:LEU573 4.5 8.1 1.0
O B:HOH1284 4.6 32.5 1.0
CA B:ASP574 4.6 6.3 1.0
N B:LEU573 4.7 5.8 1.0
C B:GLY575 4.7 13.1 1.0
C B:GLY571 4.7 8.2 1.0
N B:LEU576 4.8 10.9 1.0
N B:GLY575 4.8 12.9 1.0
CA B:GLY575 4.8 11.5 1.0
O B:LEU573 4.8 8.6 1.0
CA B:GLY571 4.9 6.7 1.0
CA B:LEU573 4.9 8.8 1.0
CB B:ASP574 5.0 10.3 1.0
CB B:LEU576 5.0 7.3 1.0
CB B:SER572 5.0 12.3 1.0

Reference:

J.L.Vanhooke, J.B.Thoden, N.M.Brunhuber, J.S.Blanchard, H.M.Holden. Phenylalanine Dehydrogenase From Rhodococcus Sp. M4: High-Resolution X-Ray Analyses of Inhibitory Ternary Complexes Reveal Key Features in the Oxidative Deamination Mechanism. Biochemistry V. 38 2326 1999.
ISSN: ISSN 0006-2960
PubMed: 10029526
DOI: 10.1021/BI982244Q
Page generated: Mon Aug 12 04:04:54 2024

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