Chlorine in PDB 1onw: Crystal Structure of Isoaspartyl Dipeptidase From E. Coli

The structure of Crystal Structure of Isoaspartyl Dipeptidase From E. Coli, PDB code: 1onw was solved by J.B.Thoden, R.Marti-Arbona, F.M.Raushel, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.65
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	116.700, 116.700, 138.500, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystal Structure of Isoaspartyl Dipeptidase From E. Coli also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	4 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Isoaspartyl Dipeptidase From E. Coli (pdb code 1onw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Isoaspartyl Dipeptidase From E. Coli, PDB code: 1onw:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Isoaspartyl Dipeptidase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Isoaspartyl Dipeptidase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl802 b:24.1 occ:1.00 O A:HOH918 3.1 23.5 1.0 O A:HOH1023 3.2 44.9 1.0 N A:LEU89 3.2 16.6 1.0 O A:HOH858 3.2 16.9 1.0 CA A:GLY385 3.5 19.2 1.0 CA A:ALA88 3.8 22.9 1.0 NZ A:LYS119 3.8 14.0 1.0 CB A:LEU89 3.9 15.7 1.0 CG A:GLU388 3.9 26.1 1.0 C A:ALA88 4.0 15.1 1.0 O A:VAL87 4.1 18.4 1.0 OE1 A:GLU388 4.1 26.6 1.0 CA A:LEU89 4.2 13.8 1.0 N A:GLY385 4.3 22.6 1.0 CD A:GLU388 4.3 24.0 1.0 O A:HOH1045 4.3 32.8 1.0 C A:GLY385 4.3 29.7 1.0 CB A:ALA88 4.4 21.5 1.0 OE2 A:GLU126 4.5 15.9 0.5 O A:HOH1070 4.5 41.9 1.0 O A:HOH971 4.7 21.7 1.0 N A:THR386 4.7 24.0 1.0 N A:ALA88 4.8 21.8 1.0 C A:VAL87 4.9 20.4 1.0 OE1 A:GLU126 4.9 15.5 0.5 OE1 A:GLU126 5.0 54.8 0.5 O A:GLY385 5.0 20.9 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Isoaspartyl Dipeptidase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Isoaspartyl Dipeptidase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:27.1 occ:1.00 N A:ASP204 3.2 28.5 1.0 N A:HIS168 3.2 18.6 1.0 CD2 A:HIS168 3.4 29.2 1.0 CA A:ASP167 3.7 13.4 1.0 CA A:ASP204 3.9 21.2 1.0 C A:ASP167 3.9 24.5 1.0 CB A:ASP204 4.0 21.5 1.0 N A:SER205 4.0 18.1 1.0 CB A:HIS168 4.0 22.0 1.0 C A:ASP204 4.1 27.3 1.0 CG A:HIS168 4.1 27.1 1.0 O A:SER166 4.1 22.5 1.0 C A:GLY203 4.1 26.8 1.0 CA A:GLY203 4.2 21.8 1.0 CA A:HIS168 4.2 22.6 1.0 OD2 A:ASP167 4.2 17.6 1.0 CG A:ASP167 4.4 22.5 1.0 CB A:ASP167 4.5 16.2 1.0 N A:ASP167 4.6 15.0 1.0 NE2 A:HIS168 4.6 30.9 1.0 C A:SER166 4.7 24.2 1.0 O A:ASP204 4.8 29.3 1.0 OD1 A:ASP167 4.8 21.8 1.0 CG A:ASP204 4.9 24.9 1.0 CA A:SER205 4.9 14.8 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Isoaspartyl Dipeptidase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Isoaspartyl Dipeptidase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl806 b:24.7 occ:1.00 N B:LEU89 3.2 17.2 1.0 O B:HOH1038 3.3 33.5 1.0 O B:HOH886 3.3 31.2 1.0 O B:HOH1044 3.4 39.0 1.0 CA B:GLY385 3.5 25.1 1.0 CA B:ALA88 3.7 15.4 1.0 NZ B:LYS119 3.8 18.7 1.0 CG B:GLU388 3.8 18.9 1.0 C B:ALA88 3.9 15.8 1.0 O B:VAL87 3.9 17.5 1.0 CB B:LEU89 4.0 11.1 1.0 OE1 B:GLU388 4.1 20.6 1.0 CA B:LEU89 4.2 15.8 1.0 CD B:GLU388 4.2 19.5 1.0 OE2 B:GLU126 4.3 21.7 0.5 N B:GLY385 4.3 26.0 1.0 C B:GLY385 4.5 21.7 1.0 CB B:ALA88 4.5 15.7 1.0 N B:ALA88 4.7 16.7 1.0 C B:VAL87 4.8 22.5 1.0 N B:THR386 4.8 20.6 1.0 OE1 B:GLU126 4.8 21.2 0.5 CD B:GLU126 4.9 22.8 0.5

J.B.Thoden, R.Marti-Arbona, F.M.Raushel, H.M.Holden. High Resolution X-Ray Structure of Isoaspartyl Dipeptidase From Escherichia Coli Biochemistry V. 42 4874 2003.
ISSN: ISSN 0006-2960
PubMed: 12718528
DOI: 10.1021/BI034233P