Potassium in PDB 1yxd: Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A

All present enzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A:
4.2.1.52;

The structure of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A, PDB code: 1yxd was solved by R.C.J.Dobson, M.D.W.Griffin, 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)	37.99 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.148, 121.148, 110.084, 90.00, 90.00, 120.00
R / Rfree (%)	15.9 / 18.6

The structure of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Potassium atom in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A (pdb code 1yxd). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A, PDB code: 1yxd:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A within 5.0Å range: probe atom residue distance (Å) B Occ A:K1301 b:26.4 occ:1.00 O A:VAL154 2.6 27.2 1.0 O A:ILE157 2.6 22.0 1.0 O A:ALA152 2.7 24.6 1.0 O A:LYS155 3.1 26.0 1.0 C A:ILE157 3.6 22.4 1.0 C A:LYS155 3.7 26.9 1.0 C A:VAL154 3.7 27.4 1.0 C A:ALA152 3.7 24.9 1.0 CA A:LYS155 4.0 27.6 1.0 N A:ILE157 4.1 23.6 1.0 N A:LYS155 4.3 27.3 1.0 CA A:ALA152 4.3 24.1 1.0 CA A:ILE157 4.4 22.4 1.0 O A:HOH1530 4.4 40.0 1.0 CG2 A:ILE158 4.5 24.7 1.0 N A:VAL154 4.5 27.3 1.0 N A:ASN156 4.5 26.3 1.0 N A:ILE158 4.6 21.9 1.0 C A:LYS153 4.6 27.8 1.0 CA A:ILE158 4.6 22.4 1.0 CA A:VAL154 4.7 27.6 1.0 N A:LYS153 4.7 25.4 1.0 C A:ASN156 4.9 24.7 1.0 CB A:ILE157 4.9 22.1 1.0 CA A:LYS153 5.0 27.5 1.0 CB A:ALA152 5.0 23.9 1.0 O A:LYS153 5.0 28.1 1.0

Potassium binding site 2 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of E. Coli Dihydrodipicolinate Synthase Bound with Allosteric Inhibitor (S)-Lysine to 2.0 A within 5.0Å range: probe atom residue distance (Å) B Occ B:K2301 b:22.1 occ:1.00 O B:ALA152 2.6 21.3 1.0 O B:ILE157 2.6 19.2 1.0 O B:VAL154 2.7 23.6 1.0 O B:HOH3498 2.8 35.7 1.0 O B:HOH3584 3.0 46.7 1.0 O B:LYS155 3.2 22.2 1.0 C B:LYS155 3.7 22.9 1.0 C B:ALA152 3.7 21.8 1.0 C B:ILE157 3.7 18.5 1.0 C B:VAL154 3.7 23.6 1.0 CA B:LYS155 4.0 23.9 1.0 N B:ILE157 4.1 19.0 1.0 N B:LYS155 4.3 23.6 1.0 O B:HOH3489 4.3 34.4 1.0 CA B:ALA152 4.3 21.2 1.0 CG2 B:ILE158 4.5 24.1 1.0 CA B:ILE157 4.5 18.7 1.0 N B:ASN156 4.5 21.3 1.0 O B:HOH3553 4.5 40.9 1.0 N B:ILE158 4.5 18.5 1.0 N B:VAL154 4.5 23.8 1.0 CA B:ILE158 4.6 19.7 1.0 C B:LYS153 4.6 23.9 1.0 N B:LYS153 4.7 22.0 1.0 CA B:VAL154 4.8 23.3 1.0 CB B:ILE157 4.9 18.3 1.0 CA B:LYS153 4.9 23.4 1.0 C B:ASN156 4.9 19.6 1.0 CB B:ALA152 5.0 21.2 1.0 O B:LYS153 5.0 23.9 1.0 CD1 B:PHE181 5.0 19.0 1.0

R.C.Dobson, M.D.Griffin, G.B.Jameson, J.A.Gerrard. The Crystal Structures of Native and (S)-Lysine-Bound Dihydrodipicolinate Synthase From Escherichia Coli with Improved Resolution Show New Features of Biological Significance. Acta Crystallogr.,Sect.D V. 61 1116 2005.
ISSN: ISSN 0907-4449
PubMed: 16041077
DOI: 10.1107/S0907444905016318