Potassium in PDB 7jz8: Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric Site

All present enzymatic activity of Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric Site:
4.3.3.7;

The structure of Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric Site, PDB code: 7jz8 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)	33.31 / 1.82
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.049, 121.049, 110.151, 90, 90, 120
R / Rfree (%)	14.3 / 17

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric Site (pdb code 7jz8). 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 Mutant S48F with Lysine in the Allosteric Site, PDB code: 7jz8:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric 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 Mutant S48F with Lysine in the Allosteric Site within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:22.7 occ:1.00 O A:HOH633 2.6 31.1 1.0 O A:ILE157 2.7 17.9 1.0 O A:VAL154 2.7 22.5 1.0 O A:ALA152 2.7 20.8 1.0 O A:HOH645 2.9 46.5 1.0 O A:LYS155 3.1 20.2 1.0 C A:LYS155 3.7 23.8 1.0 C A:ILE157 3.7 17.5 1.0 C A:VAL154 3.7 20.4 1.0 C A:ALA152 3.8 19.6 1.0 CA A:LYS155 4.0 25.7 1.0 N A:ILE157 4.1 17.6 1.0 O A:HOH609 4.2 40.3 1.0 N A:LYS155 4.3 22.3 1.0 CA A:ILE157 4.4 16.9 1.0 CA A:ALA152 4.4 17.6 1.0 N A:VAL154 4.6 21.5 1.0 N A:ASN156 4.6 19.9 1.0 N A:ILE158 4.6 16.2 1.0 CA A:ILE158 4.6 18.6 1.0 C A:LYS153 4.7 27.0 1.0 CG2 A:ILE158 4.7 24.0 1.0 N A:LYS153 4.8 17.4 1.0 CA A:VAL154 4.8 21.8 1.0 C A:ASN156 4.9 19.4 1.0 CB A:ILE157 4.9 16.6 1.0 CA A:LYS153 5.0 22.9 1.0 CD1 A:PHE181 5.0 19.1 1.0

Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase Mutant S48F with Lysine in the Allosteric 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 Mutant S48F with Lysine in the Allosteric Site within 5.0Å range: probe atom residue distance (Å) B Occ B:K301 b:18.0 occ:1.00 O B:ILE157 2.7 12.3 1.0 O B:VAL154 2.7 20.8 1.0 O B:ALA152 2.7 14.9 1.0 O B:HOH654 2.7 28.6 1.0 O B:HOH658 2.8 44.7 1.0 O B:LYS155 3.2 17.1 1.0 C B:LYS155 3.7 18.2 1.0 C B:ILE157 3.7 13.0 1.0 C B:VAL154 3.7 20.8 1.0 C B:ALA152 3.7 15.0 1.0 O B:HOH597 4.0 38.1 1.0 CA B:LYS155 4.0 20.3 1.0 N B:ILE157 4.1 12.6 1.0 N B:LYS155 4.3 19.3 1.0 CA B:ALA152 4.4 13.5 1.0 CA B:ILE157 4.5 12.7 1.0 O B:HOH656 4.5 41.9 1.0 N B:ASN156 4.6 14.7 1.0 N B:VAL154 4.6 19.9 1.0 C B:LYS153 4.6 21.0 1.0 N B:ILE158 4.6 12.2 1.0 CA B:ILE158 4.7 14.4 1.0 N B:LYS153 4.8 15.2 1.0 CA B:VAL154 4.8 19.7 1.0 O B:LYS153 4.9 19.2 1.0 CD1 B:PHE181 4.9 12.6 1.0 CA B:LYS153 4.9 16.9 1.0 CG2 B:ILE158 4.9 25.7 1.0 CB B:ILE157 5.0 12.9 1.0 C B:ASN156 5.0 13.1 1.0

A.J.Board, R.C.J.Dobson. Mapping the Unchartered Waters of Dihydrodipicolinate Synthase: A Novel Mechanism of Allosteric Inhibition. To Be Published.