Potassium in PDB 2a6n: Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A

All present enzymatic activity of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A:
4.2.1.52;

The structure of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A, PDB code: 2a6n was solved by R.C.Dobson, S.R.Devenish, L.A.Turner, V.R.Clifford, F.G.Pearce, 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)	33.33 / 1.94
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.989, 120.989, 111.302, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 19.1

The binding sites of Potassium atom in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A (pdb code 2a6n). 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 (E. Coli)- Mutant R138A, PDB code: 2a6n:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A within 5.0Å range: probe atom residue distance (Å) B Occ A:K600 b:28.5 occ:1.00 O A:VAL154 2.6 29.3 1.0 O A:ILE157 2.6 23.8 1.0 O A:ALA152 2.7 25.0 1.0 O A:HOH787 2.8 39.0 1.0 O A:LYS155 3.1 29.1 1.0 C A:ILE157 3.7 24.2 1.0 C A:VAL154 3.7 29.3 1.0 C A:LYS155 3.7 29.3 1.0 C A:ALA152 3.8 25.2 1.0 CA A:LYS155 4.0 30.1 1.0 N A:ILE157 4.2 25.6 1.0 N A:LYS155 4.3 30.0 1.0 CA A:ALA152 4.4 24.1 1.0 CA A:ILE157 4.5 24.6 1.0 O A:HOH831 4.5 42.3 1.0 O A:HOH847 4.5 44.7 1.0 N A:VAL154 4.5 28.6 1.0 CG2 A:ILE158 4.5 26.9 1.0 N A:ILE158 4.6 23.6 1.0 CA A:ILE158 4.6 24.0 1.0 C A:LYS153 4.6 28.2 1.0 N A:ASN156 4.6 28.3 1.0 N A:LYS153 4.8 25.6 1.0 CA A:VAL154 4.8 29.1 1.0 CB A:ILE157 4.9 24.5 1.0 O A:LYS153 4.9 28.5 1.0 CD1 A:PHE181 4.9 25.1 1.0 CA A:LYS153 4.9 27.5 1.0

Potassium binding site 2 out of 2 in the Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Dihydrodipicolinate Synthase (E. Coli)- Mutant R138A within 5.0Å range: probe atom residue distance (Å) B Occ B:K601 b:24.8 occ:1.00 O B:ILE157 2.6 20.4 1.0 O B:VAL154 2.7 25.9 1.0 O B:ALA152 2.7 21.3 1.0 O B:HOH744 2.7 31.8 1.0 O B:HOH914 3.0 47.7 1.0 O B:LYS155 3.2 23.9 1.0 C B:VAL154 3.7 26.0 1.0 C B:ILE157 3.7 20.0 1.0 C B:LYS155 3.7 25.0 1.0 C B:ALA152 3.7 21.6 1.0 CA B:LYS155 4.1 26.0 1.0 N B:ILE157 4.2 20.5 1.0 O B:HOH867 4.2 42.1 1.0 N B:LYS155 4.3 25.9 1.0 CA B:ALA152 4.4 20.5 1.0 CA B:ILE157 4.5 20.1 1.0 N B:VAL154 4.5 25.4 1.0 C B:LYS153 4.6 25.4 1.0 N B:ASN156 4.6 23.2 1.0 N B:ILE158 4.6 19.3 1.0 CA B:ILE158 4.7 19.8 1.0 N B:LYS153 4.7 22.8 1.0 CA B:VAL154 4.8 25.7 1.0 CD1 B:PHE181 4.8 18.8 1.0 O B:LYS153 4.9 25.8 1.0 CA B:LYS153 4.9 24.5 1.0 CB B:ILE157 4.9 19.6 1.0 C B:ASN156 5.0 20.9 1.0

R.C.Dobson, S.R.Devenish, L.A.Turner, V.R.Clifford, F.G.Pearce, G.B.Jameson, J.A.Gerrard. Role of Arginine 138 in the Catalysis and Regulation of Escherichia Coli Dihydrodipicolinate Synthase. Biochemistry V. 44 13007 2005.
ISSN: ISSN 0006-2960
PubMed: 16185069
DOI: 10.1021/BI051281W