Potassium in PDB 2pur: Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A.

All present enzymatic activity of Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A.:
4.2.1.52;

The structure of Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A., PDB code: 2pur was solved by 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)	33.31 / 1.70
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	121.040, 121.040, 110.319, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 20.7

The binding sites of Potassium atom in the Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A. (pdb code 2pur). 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 Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A., PDB code: 2pur:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 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 Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:K801 b:33.8 occ:1.00 O A:ILE157 2.7 29.5 1.0 O A:VAL154 2.7 33.2 1.0 O A:HOH985 2.7 44.9 1.0 O A:ALA152 2.7 31.6 1.0 O A:LYS155 3.1 34.1 1.0 C A:LYS155 3.7 34.1 1.0 C A:ILE157 3.7 30.1 1.0 C A:VAL154 3.7 33.8 1.0 C A:ALA152 3.8 30.8 1.0 CA A:LYS155 4.0 35.1 1.0 N A:ILE157 4.2 30.9 1.0 O A:HOH1053 4.3 48.8 1.0 N A:LYS155 4.3 34.4 1.0 CA A:ALA152 4.4 29.9 1.0 CA A:ILE157 4.5 30.7 1.0 CG2 A:ILE158 4.5 32.9 1.0 N A:VAL154 4.6 33.4 1.0 N A:ILE158 4.6 29.9 1.0 CA A:ILE158 4.6 30.1 1.0 N A:ASN156 4.6 32.9 1.0 C A:LYS153 4.7 33.5 1.0 CA A:VAL154 4.8 33.6 1.0 N A:LYS153 4.8 31.3 1.0 CB A:ILE157 4.9 30.3 1.0 O A:LYS153 5.0 34.3 1.0 CD1 A:PHE181 5.0 32.9 1.0 C A:ASN156 5.0 31.7 1.0

Potassium binding site 2 out of 2 in the Structure of Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 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 Dihydrodipicolinate Synthase Mutant THR44SER at 1.7 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:K802 b:31.6 occ:1.00 O B:VAL154 2.6 31.2 1.0 O B:ALA152 2.6 27.6 1.0 O B:ILE157 2.7 25.7 1.0 O B:HOH994 2.7 40.3 1.0 O B:LYS155 3.2 29.8 1.0 O B:HOH1117 3.5 54.4 1.0 C B:VAL154 3.6 31.4 1.0 C B:LYS155 3.7 30.4 1.0 C B:ALA152 3.7 27.4 1.0 C B:ILE157 3.7 25.9 1.0 CA B:LYS155 4.0 31.2 1.0 N B:ILE157 4.2 26.5 1.0 N B:LYS155 4.2 31.5 1.0 CA B:ALA152 4.4 26.7 1.0 O B:HOH1114 4.4 54.4 1.0 N B:VAL154 4.5 31.1 1.0 CA B:ILE157 4.5 26.1 1.0 N B:ASN156 4.6 28.0 1.0 C B:LYS153 4.6 31.4 1.0 N B:ILE158 4.6 25.1 1.0 CA B:ILE158 4.7 25.9 1.0 N B:LYS153 4.7 28.9 1.0 CA B:VAL154 4.7 31.2 1.0 O B:HOH1170 4.8 52.4 1.0 CA B:LYS153 4.9 30.5 1.0 CD1 B:PHE181 4.9 25.7 1.0 O B:LYS153 4.9 31.4 1.0 CB B:ILE157 5.0 26.2 1.0

R.C.Dobson, M.A.Perugini, G.B.Jameson, J.A.Gerrard. Specificity Versus Catalytic Potency: the Role of Threonine 44 in Escherichia Coli Dihydrodipicolinate Synthase Mediated Catalysis. Biochimie V. 91 1036 2009.
ISSN: ISSN 0300-9084
PubMed: 19505526
DOI: 10.1016/J.BIOCHI.2009.05.013