Potassium in PDB 2ats: Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine

All present enzymatic activity of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine:
4.2.1.52;

The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine, PDB code: 2ats was solved by S.R.A.Devenish, R.C.J.Dobson, G.B.Jameson, J.A.Gerrard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.80 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.680, 121.680, 109.799, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 20.2

The structure of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine (pdb code 2ats). 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 Co-Crystallised with (S)-Lysine, PDB code: 2ats:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:24.7 occ:1.00 O A:ALA152 2.7 22.6 1.0 O A:ILE157 2.7 20.8 1.0 O A:VAL154 2.7 24.8 1.0 O A:HOH3177 2.8 33.9 1.0 O A:HOH3276 3.0 44.0 1.0 O A:LYS155 3.1 24.1 1.0 C A:ILE157 3.7 19.9 1.0 C A:LYS155 3.7 24.0 1.0 C A:VAL154 3.7 24.7 1.0 C A:ALA152 3.7 22.5 1.0 CA A:LYS155 4.0 25.0 1.0 O A:HOH3277 4.1 45.2 1.0 N A:ILE157 4.2 21.1 1.0 N A:LYS155 4.3 24.6 1.0 CA A:ALA152 4.4 21.7 1.0 O A:HOH3230 4.4 39.8 1.0 CA A:ILE157 4.4 20.4 1.0 CG2 A:ILE158 4.5 21.2 1.0 N A:VAL154 4.5 25.2 1.0 N A:ILE158 4.6 19.6 1.0 C A:LYS153 4.6 25.3 1.0 N A:ASN156 4.6 23.0 1.0 CA A:ILE158 4.6 19.8 1.0 N A:LYS153 4.7 23.0 1.0 CA A:VAL154 4.8 25.2 1.0 CB A:ILE157 4.9 20.8 1.0 O A:LYS153 4.9 25.9 1.0 CA A:LYS153 4.9 24.7 1.0 C A:ASN156 5.0 21.7 1.0 CB A:ALA152 5.0 21.5 1.0 CD1 A:PHE181 5.0 22.6 1.0

Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase Co-Crystallised with (S)-Lysine within 5.0Å range: probe atom residue distance (Å) B Occ B:K1002 b:20.8 occ:1.00 O B:ILE157 2.6 17.2 1.0 O B:ALA152 2.7 19.2 1.0 O B:VAL154 2.7 22.2 1.0 O B:HOH2162 2.7 30.4 1.0 O B:HOH2295 2.9 44.0 1.0 O B:LYS155 3.1 19.4 1.0 C B:ILE157 3.7 17.4 1.0 C B:LYS155 3.7 20.8 1.0 C B:ALA152 3.7 19.4 1.0 C B:VAL154 3.7 22.2 1.0 CA B:LYS155 4.0 21.6 1.0 O B:HOH2210 4.0 36.3 1.0 N B:ILE157 4.1 18.1 1.0 N B:LYS155 4.3 21.9 1.0 CA B:ALA152 4.4 19.0 1.0 CA B:ILE157 4.4 17.5 1.0 O B:HOH2261 4.5 39.8 1.0 N B:ILE158 4.5 17.1 1.0 CA B:ILE158 4.6 17.9 1.0 N B:VAL154 4.6 21.8 1.0 N B:ASN156 4.6 19.5 1.0 CG2 B:ILE158 4.6 20.1 1.0 C B:LYS153 4.6 21.7 1.0 N B:LYS153 4.7 20.1 1.0 CA B:VAL154 4.8 21.7 1.0 CD1 B:PHE181 4.9 16.4 1.0 CB B:ILE157 4.9 16.9 1.0 CA B:LYS153 4.9 21.0 1.0 O B:LYS153 4.9 22.0 1.0 C B:ASN156 4.9 18.2 1.0

S.R.A.Devenish, R.C.J.Dobson, G.B.Jameson, J.A.Gerrard. The Co-Crystallisation of (S)-Lysine-Bound Dihydrodipicolinate Synthase From E. Coli Indicates That Domain Movements Are Not Responsible For (S)-Lysine Inhibition To Be Published.