Potassium in PDB 1c1x: L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate

The structure of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate, PDB code: 1c1x was solved by J.L.Vanhooke, J.B.Thoden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.600, 110.400, 113.400, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Potassium atom in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate (pdb code 1c1x). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate, PDB code: 1c1x:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate within 5.0Å range: probe atom residue distance (Å) B Occ A:K850 b:28.8 occ:1.00 O A:THR121 2.7 23.0 1.0 O A:ASP118 2.7 16.9 1.0 O A:HOH1574 2.8 45.9 1.0 O A:HOH1488 2.9 32.2 1.0 O A:HOH1650 3.1 51.5 1.0 O A:HOH1583 3.2 35.5 1.0 O A:HOH1582 3.2 50.4 1.0 O A:HOH1159 3.3 30.9 1.0 C A:ASP118 3.7 16.2 1.0 C A:THR121 3.9 23.9 1.0 N A:ASP118 4.0 14.0 1.0 CA A:ASP118 4.2 14.8 1.0 CB A:PRO117 4.2 16.6 1.0 N A:THR121 4.3 13.3 1.0 O A:HOH1600 4.4 43.9 1.0 C A:PRO117 4.5 16.3 1.0 CA A:ASN122 4.6 15.7 1.0 O1N A:NAD360 4.6 28.9 1.0 N A:VAL119 4.7 12.7 1.0 N A:ASN122 4.7 18.2 1.0 N A:ASN120 4.8 17.6 1.0 CA A:THR121 4.8 12.0 1.0 O A:HOH1587 4.8 43.0 1.0 CA A:VAL119 4.9 15.1 1.0 CA A:PRO117 4.9 18.7 1.0

Potassium binding site 2 out of 4 in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate within 5.0Å range: probe atom residue distance (Å) B Occ A:K853 b:35.2 occ:1.00 O A:TRP8 2.7 19.0 1.0 O A:GLY10 2.7 12.6 1.0 O A:HOH1868 2.9 32.0 1.0 C A:TRP8 3.6 13.6 1.0 N A:GLY10 3.6 12.9 1.0 C A:GLY10 3.7 10.8 1.0 C A:ASP9 3.9 15.5 1.0 CE3 A:TRP8 3.9 10.7 1.0 O A:HOH1226 4.1 29.8 1.0 CA A:ASP9 4.1 16.8 1.0 CA A:GLY10 4.2 12.2 1.0 N A:ASP9 4.2 14.0 1.0 O A:ASP9 4.5 16.2 1.0 CA A:TRP8 4.5 14.8 1.0 CZ3 A:TRP8 4.6 12.8 1.0 CB A:TRP8 4.6 15.3 1.0 CD2 A:TRP8 4.7 11.8 1.0 N A:GLU11 4.8 11.1 1.0 C A:GLU11 4.9 18.4 1.0 N A:TRP8 4.9 23.4 1.0 N A:MET12 5.0 11.9 1.0 CG A:TRP8 5.0 17.2 1.0

Potassium binding site 3 out of 4 in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate within 5.0Å range: probe atom residue distance (Å) B Occ B:K851 b:22.8 occ:1.00 O B:SER172 2.6 12.0 1.0 O B:ASP174 2.6 19.3 1.0 O B:HOH1187 2.6 24.1 1.0 O B:HOH1408 2.9 27.4 1.0 O B:LEU170 3.1 15.7 1.0 CD2 B:LEU176 3.5 11.0 1.0 CG B:LEU176 3.7 12.6 1.0 C B:SER172 3.7 11.8 1.0 C B:ASP174 3.8 15.2 1.0 N B:SER172 3.8 14.2 1.0 N B:ASP174 4.3 15.8 1.0 OG B:SER172 4.4 24.1 1.0 CA B:SER172 4.4 16.5 1.0 C B:LEU170 4.4 16.2 1.0 CD1 B:LEU176 4.4 14.3 1.0 C B:LEU173 4.5 16.2 1.0 CA B:ASP174 4.6 11.4 1.0 C B:GLY175 4.6 39.3 1.0 N B:LEU176 4.7 17.9 1.0 C B:GLY171 4.7 13.2 1.0 N B:LEU173 4.7 12.8 1.0 N B:GLY175 4.8 15.4 1.0 CA B:GLY175 4.8 20.3 1.0 O B:LEU173 4.9 13.4 1.0 O B:GLY175 4.9 32.9 1.0 CA B:GLY171 4.9 11.3 1.0 CA B:LEU173 4.9 15.0 1.0 CB B:ASP174 5.0 13.8 1.0 CB B:LEU176 5.0 12.7 1.0

Potassium binding site 4 out of 4 in the L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of L-Phenylalanine Dehydrogenase Structure in Ternary Complex with Nad+ and L-3-Phenyllactate within 5.0Å range: probe atom residue distance (Å) B Occ B:K852 b:25.1 occ:1.00 O B:THR121 2.6 16.6 1.0 O B:ASP118 2.7 14.8 1.0 O B:HOH1645 2.7 36.9 1.0 O B:HOH1511 3.0 42.7 1.0 O B:HOH1762 3.0 35.7 1.0 O B:HOH1077 3.6 27.2 1.0 C B:ASP118 3.7 15.5 1.0 C B:THR121 3.8 13.8 1.0 N B:ASP118 4.1 11.8 1.0 N B:THR121 4.2 11.1 1.0 CB B:PRO117 4.3 15.1 1.0 CA B:ASP118 4.3 10.2 1.0 CA B:ASN122 4.6 11.9 1.0 O B:HOH1618 4.6 41.9 1.0 N B:ASN120 4.6 12.8 1.0 N B:ASN122 4.6 12.0 1.0 N B:VAL119 4.7 13.6 1.0 CA B:THR121 4.7 10.4 1.0 O1N B:NAD760 4.7 23.6 0.6 C B:PRO117 4.7 11.6 1.0 O B:HOH1436 4.8 34.7 1.0 CA B:VAL119 4.8 13.7 1.0 CB B:ASN122 5.0 13.4 1.0

N.M.Brunhuber, J.B.Thoden, J.S.Blanchard, J.L.Vanhooke. Rhodococcus L-Phenylalanine Dehydrogenase: Kinetics, Mechanism, and Structural Basis For Catalytic Specificity. Biochemistry V. 39 9174 2000.
ISSN: ISSN 0006-2960
PubMed: 10924111
DOI: 10.1021/BI000494C