Potassium in PDB 7jzc: Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site

All present enzymatic activity of Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site:
4.3.3.7;

The structure of Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site, PDB code: 7jzc was solved by A.J.Board, R.C.J.Dobson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.65 / 2.07
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.129, 121.129, 111.271, 90, 90, 120
R / Rfree (%)	17.2 / 20.9

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site (pdb code 7jzc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site, PDB code: 7jzc:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:40.9 occ:1.00 O A:HOH495 2.1 53.2 1.0 O A:VAL154 2.5 33.5 1.0 O A:ILE157 2.7 36.2 1.0 O A:ALA152 2.8 36.0 1.0 O A:LYS155 2.9 42.1 1.0 C A:VAL154 3.6 39.1 1.0 C A:LYS155 3.6 43.3 1.0 C A:ILE157 3.7 30.9 1.0 C A:ALA152 3.8 37.9 1.0 N A:ILE157 4.0 36.0 1.0 CA A:LYS155 4.0 42.8 1.0 N A:LYS155 4.3 40.0 1.0 CA A:ILE157 4.3 34.1 1.0 CA A:ALA152 4.4 35.7 1.0 N A:VAL154 4.4 42.8 1.0 N A:ASN156 4.5 36.9 1.0 C A:LYS153 4.5 46.2 1.0 CA A:VAL154 4.6 39.5 1.0 N A:ILE158 4.6 29.9 1.0 CA A:ILE158 4.7 31.2 1.0 N A:LYS153 4.7 38.9 1.0 O A:LYS153 4.7 45.4 1.0 CG2 A:ILE158 4.7 37.7 1.0 CB A:ILE157 4.8 32.1 1.0 C A:ASN156 4.8 36.7 1.0 CA A:LYS153 4.9 45.5 1.0 O A:LEU151 4.9 32.8 1.0 CA A:ASN156 5.0 39.9 1.0

Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase S48W Mutant with Lysine in the Allosteric Site, and Pyruvate in the Catalytic Site within 5.0Å range: probe atom residue distance (Å) B Occ B:K301 b:31.4 occ:1.00 O B:ALA152 2.6 26.3 1.0 O B:VAL154 2.6 32.1 1.0 O B:HOH536 2.7 44.6 1.0 O B:ILE157 2.7 23.0 1.0 O B:HOH535 2.7 44.3 1.0 O B:LYS155 3.2 35.2 1.0 C B:ALA152 3.7 26.9 1.0 C B:VAL154 3.7 35.1 1.0 C B:LYS155 3.7 38.6 1.0 C B:ILE157 3.8 22.7 1.0 CA B:LYS155 4.0 39.5 1.0 N B:ILE157 4.2 26.1 1.0 CA B:ALA152 4.3 25.4 1.0 N B:LYS155 4.3 38.4 1.0 N B:VAL154 4.5 34.5 1.0 CA B:ILE157 4.5 23.8 1.0 N B:ASN156 4.6 28.6 1.0 C B:LYS153 4.6 33.4 1.0 CA B:ILE158 4.6 22.9 1.0 N B:ILE158 4.6 21.8 1.0 N B:LYS153 4.7 28.0 1.0 CA B:VAL154 4.8 32.9 1.0 CB B:ILE157 4.9 23.0 1.0 CD1 B:PHE181 4.9 22.4 1.0 CA B:LYS153 4.9 31.8 1.0 C B:ASN156 4.9 27.2 1.0 CB B:ALA152 5.0 26.9 1.0 O B:LYS153 5.0 33.9 1.0 O B:LEU151 5.0 23.0 1.0 CG2 B:ILE158 5.0 30.8 1.0

A.J.Board, R.C.J.Dobson. Mapping the Uncharted Water Channel of Dhdps To Be Published.