Potassium in PDB 3c0j: Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate

All present enzymatic activity of Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate:
4.2.1.52;

The structure of Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate, PDB code: 3c0j was solved by R.C.J.Dobson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.49 / 2.40
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.967, 120.967, 110.639, 90.00, 90.00, 120.00
R / Rfree (%)	17 / 23.7

The binding sites of Potassium atom in the Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate (pdb code 3c0j). 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 Complexed with Hydroxypyruvate, PDB code: 3c0j:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate


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 Complexed with Hydroxypyruvate within 5.0Å range: probe atom residue distance (Å) B Occ A:K293 b:43.0 occ:1.00 O A:ALA152 2.7 38.7 1.0 O A:VAL154 2.7 43.1 1.0 O A:ILE157 2.7 38.1 1.0 O A:HOH398 2.9 48.7 1.0 O A:HOH532 3.0 58.4 1.0 O A:LYS155 3.4 42.7 1.0 C A:ILE157 3.7 38.3 1.0 C A:ALA152 3.7 39.1 1.0 C A:VAL154 3.8 42.5 1.0 O A:HOH516 3.8 59.0 1.0 C A:LYS155 3.9 42.5 1.0 N A:ILE157 4.2 38.1 1.0 CA A:LYS155 4.2 43.4 1.0 CA A:ALA152 4.3 38.5 1.0 O A:HOH496 4.3 58.3 1.0 N A:LYS155 4.4 43.1 1.0 CA A:ILE157 4.5 38.2 1.0 N A:ILE158 4.6 38.5 1.0 CA A:ILE158 4.6 38.9 1.0 C A:LYS153 4.6 42.8 1.0 N A:VAL154 4.7 42.9 1.0 N A:ASN156 4.7 41.5 1.0 N A:LYS153 4.7 40.2 1.0 CD1 A:PHE181 4.8 37.3 1.0 CA A:VAL154 4.8 41.5 1.0 CA A:LYS153 4.9 42.2 1.0 O A:LYS153 4.9 43.4 1.0 CG2 A:ILE158 4.9 38.6 1.0 CB A:ALA152 4.9 37.8 1.0 CB A:ILE157 5.0 38.2 1.0

Potassium binding site 2 out of 2 in the Structure of E. Coli Dihydrodipicolinate Synthase Complexed with Hydroxypyruvate


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 Complexed with Hydroxypyruvate within 5.0Å range: probe atom residue distance (Å) B Occ B:K293 b:50.0 occ:1.00 O B:VAL154 2.5 47.1 1.0 O B:ILE157 2.6 40.5 1.0 O B:ALA152 2.7 42.9 1.0 O B:LYS155 3.2 48.3 1.0 C B:VAL154 3.7 47.4 1.0 C B:ILE157 3.7 40.5 1.0 C B:ALA152 3.7 43.3 1.0 C B:LYS155 3.8 48.8 1.0 CA B:LYS155 4.1 49.6 1.0 N B:ILE157 4.2 43.3 1.0 N B:LYS155 4.3 48.9 1.0 CA B:ALA152 4.3 42.9 1.0 O B:HOH462 4.4 54.8 1.0 CG2 B:ILE158 4.4 38.9 1.0 CA B:ILE157 4.4 41.6 1.0 N B:ILE158 4.5 40.8 1.0 CA B:ILE158 4.6 40.3 1.0 N B:VAL154 4.6 46.1 1.0 C B:LYS153 4.7 45.9 1.0 N B:ASN156 4.8 47.8 1.0 CA B:VAL154 4.8 45.9 1.0 N B:LYS153 4.8 44.0 1.0 CB B:ILE157 4.8 41.0 1.0 CD1 B:PHE181 4.9 47.5 1.0 CA B:LYS153 5.0 45.8 1.0 CB B:ALA152 5.0 41.2 1.0 O B:LYS153 5.0 46.3 1.0

R.C.J.Dobson, M.D.W.Griffin, S.R.A.Devenish, F.G.Pearce, C.A.Hutton, J.A.Gerrard, G.B.Jameson, M.A.Perugini. Conserved Main-Chain Peptide Distortions: A Proposed Role For ILE203 in Catalysis By Dihydrodipicolinate Synthase Protein Sci. V. 17 2080 2008.
ISSN: ISSN 0961-8368
PubMed: 18787203
DOI: 10.1110/PS.037440.108