Chlorine in PDB 4r53: Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site

All present enzymatic activity of Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site:
4.3.3.7;

The structure of Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site, PDB code: 4r53 was solved by C.J.T.Conly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.02 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.220, 97.560, 82.400, 90.00, 109.47, 90.00
R / Rfree (%)	17.4 / 21.3

The binding sites of Chlorine atom in the Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site (pdb code 4r53). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site, PDB code: 4r53:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:41.1 occ:1.00 O B:HOH523 2.8 39.7 1.0 N B:THR47 3.1 21.0 1.0 OG1 B:THR48 3.2 15.3 1.0 N B:THR48 3.3 17.9 1.0 NZ B:LYS166 3.5 19.8 1.0 CB B:THR47 3.6 23.8 1.0 CB B:ALA12 3.7 14.2 1.0 CA B:THR47 3.7 20.6 1.0 OG1 B:THR47 3.9 28.3 1.0 CB B:THR48 3.9 16.8 1.0 C B:GLY46 3.9 21.9 1.0 C B:THR47 4.0 19.0 1.0 CA B:GLY46 4.1 22.3 1.0 CA B:THR48 4.2 19.2 1.0 OH B:TYR137 4.2 24.5 1.0 O B:HOH411 4.8 15.3 1.0 CE2 B:TYR137 4.9 20.1 1.0 CZ B:TYR137 4.9 21.6 1.0 O B:GLY46 4.9 23.4 1.0 CE B:LYS166 4.9 17.9 1.0 CA B:ALA12 5.0 16.3 1.0

Chlorine binding site 2 out of 2 in the Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Dihydrodipicolinate Synthase From C. Jejuni with Vacant Active Site and Vacant Allosteric Site within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl302 b:48.4 occ:1.00 O D:HOH497 2.8 31.2 1.0 NZ D:LYS166 3.3 16.8 1.0 N D:THR47 3.3 19.1 1.0 OG1 D:THR48 3.4 13.2 1.0 N D:THR48 3.5 14.8 1.0 CB D:ALA12 3.7 10.0 1.0 CB D:THR47 3.8 25.0 1.0 OG1 D:THR47 3.9 27.5 1.0 CA D:THR47 4.0 18.4 1.0 OH D:TYR137 4.0 22.4 1.0 C D:GLY46 4.1 16.6 1.0 CB D:THR48 4.1 12.2 1.0 CA D:GLY46 4.2 14.7 1.0 C D:THR47 4.3 15.4 1.0 CA D:THR48 4.5 14.9 1.0 CE2 D:TYR137 4.6 17.9 1.0 CZ D:TYR137 4.6 19.0 1.0 CE D:LYS166 4.7 14.2 1.0 O D:HOH412 4.9 10.7 1.0

C.J.Conly, Y.V.Skovpen, S.Li, D.R.Palmer, D.A.Sanders. Tyrosine 110 Plays A Critical Role in Regulating the Allosteric Inhibition of Campylobacter Jejuni Dihydrodipicolinate Synthase By Lysine. Biochemistry V. 53 7396 2014.
ISSN: ISSN 0006-2960
PubMed: 25369463
DOI: 10.1021/BI5012157