Sodium in PDB 6nva: Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161.

All present enzymatic activity of Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161.:
4.3.3.7;

The structure of Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161., PDB code: 6nva was solved by L.M.Thomas, L.Chooback, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.17 / 2.16
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	86.140, 86.333, 107.002, 109.72, 104.24, 99.18
R / Rfree (%)	18.3 / 23.9

The binding sites of Sodium atom in the Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161. (pdb code 6nva). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161., PDB code: 6nva:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161. within 5.0Å range: probe atom residue distance (Å) B Occ C:Na302 b:36.9 occ:1.00 O C:ALA152 2.6 21.6 1.0 O C:ILE157 2.7 24.9 1.0 O C:VAL154 2.9 32.0 1.0 O C:LYS155 3.5 32.0 1.0 C C:ALA152 3.7 26.2 1.0 C C:ILE157 3.7 21.9 1.0 C C:VAL154 4.0 34.3 1.0 O C:HOH470 4.0 31.6 1.0 C C:LYS155 4.2 37.0 1.0 N C:ILE157 4.3 24.7 1.0 CA C:ALA152 4.5 24.6 1.0 CA C:ILE158 4.6 21.3 1.0 CA C:ILE157 4.6 23.6 1.0 N C:ILE158 4.6 19.8 1.0 C C:LYS153 4.6 28.5 1.0 O C:HOH619 4.6 42.6 1.0 N C:VAL154 4.7 36.6 1.0 CG2 C:ILE158 4.7 24.5 1.0 N C:LYS153 4.7 26.5 1.0 CA C:LYS155 4.7 36.8 1.0 N C:LYS155 4.7 34.2 1.0 CA C:LYS153 4.9 30.4 1.0 CD1 C:PHE181 4.9 22.7 1.0 N C:ASN156 5.0 28.2 1.0 O C:LYS153 5.0 34.5 1.0 CB C:ILE157 5.0 21.5 1.0 CA C:VAL154 5.0 33.5 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161. within 5.0Å range: probe atom residue distance (Å) B Occ F:Na302 b:19.6 occ:1.00 OG F:SER185 2.7 16.7 1.0 OG F:SER190 2.7 12.0 1.0 O F:HOH503 2.8 17.2 1.0 CD2 F:PHE194 3.3 20.4 1.0 CB F:SER185 3.4 12.6 1.0 O F:SER190 3.5 15.7 1.0 CB F:PHE194 3.6 18.1 1.0 C F:SER190 3.7 18.0 1.0 O F:ASP187 3.7 16.8 1.0 CG F:PHE194 3.8 17.7 1.0 CB F:SER190 3.9 13.4 1.0 N F:ALA191 4.1 18.0 1.0 CB F:ASP187 4.2 19.2 1.0 CA F:ALA191 4.2 17.8 1.0 CD2 F:LEU167 4.2 11.5 1.0 CA F:SER185 4.2 14.1 1.0 CE2 F:PHE194 4.2 13.8 1.0 N F:ASP187 4.3 18.5 1.0 CA F:SER190 4.3 14.9 1.0 O F:GLU162 4.4 17.0 1.0 C F:ASP187 4.6 17.2 1.0 CA F:ASP187 4.6 18.6 1.0 CA F:GLY165 4.6 18.6 1.0 N F:GLY186 4.6 16.3 1.0 OD2 F:ASP187 4.6 19.4 1.0 CA F:PHE194 4.8 18.9 1.0 C F:SER185 4.9 18.3 1.0 N F:SER190 4.9 16.1 1.0 CD1 F:PHE194 4.9 20.3 1.0 CG F:ASP187 5.0 21.2 1.0 N F:GLY165 5.0 17.1 1.0

L.Chooback, L.M.Thomas, W.Karsten, F.Sultana, S.Mesiya. Crystal Structure of Escherichia Coli Dihydrodipicolinate Synthase and Propionate Covalently Bound to K161. To Be Published.