Chlorine in PDB 7p1o: Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid

The structure of Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid, PDB code: 7p1o was solved by T.M.Gloster, S.A.Mcmahon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	92.72 / 1.60
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.123, 66.832, 92.73, 90, 90.89, 90
R / Rfree (%)	15.5 / 18.4

The binding sites of Chlorine atom in the Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid (pdb code 7p1o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid, PDB code: 7p1o:

Chlorine binding site 1 out of 1 in the Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto- 3-Deoxynononic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:21.1 occ:1.00 OH X:TYR132 3.0 14.0 1.0 O X:HOH847 3.1 19.1 1.0 N A:GLY241 3.3 13.3 1.0 NH2 A:ARG238 3.3 24.0 1.0 O X:HOH662 3.8 19.1 1.0 CE1 X:TYR132 3.8 13.7 1.0 CA A:ASN240 3.8 13.5 1.0 C2 X:GOL501 3.8 28.1 1.0 CZ X:TYR132 3.8 13.7 1.0 C3 X:GOL501 3.9 28.4 1.0 C A:ASN240 4.0 13.2 1.0 NH1 A:ARG238 4.1 24.6 1.0 CB A:ASN240 4.1 14.2 1.0 CZ A:ARG238 4.1 23.9 1.0 C1 X:GOL501 4.2 26.7 1.0 CA A:GLY241 4.2 13.7 1.0 O1 X:GOL501 4.4 25.6 1.0 O3 X:GOL501 4.5 28.6 1.0 CG2 X:THR130 4.5 15.2 1.0 CG2 X:THR173 4.6 10.8 0.5 O X:HOH622 4.7 15.2 1.0 O A:HOH923 4.8 29.4 1.0 O A:LEU239 5.0 15.6 1.0

T.M.Gloster, S.A.Mcmahon. Structure of Kdnase From Aspergillus Terrerus in Complex with 2-Keto-3-Deoxynononic Acid To Be Published.