Chlorine in PDB 1r6o: Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps

The structure of Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps, PDB code: 1r6o was solved by D.Xia, M.R.Maurizi, F.Guo, S.K.Singh, L.Esser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.25
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.436, 87.436, 212.955, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 20.5

The structure of Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps also contains other interesting chemical elements:

Yttrium	(Y)	6 atoms
Zinc	(Zn)	2 atoms

The binding sites of Chlorine atom in the Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps (pdb code 1r6o). 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 Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps, PDB code: 1r6o:

Chlorine binding site 1 out of 1 in the Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Atp-Dependent Clp Protease Atp-Binding Subunit Clpa/Atp-Dependent Clp Protease Adaptor Protein Clps within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl144 b:43.0 occ:1.00 O B:HOH422 3.0 44.4 1.0 N B:GLY105 3.1 27.1 1.0 ND2 B:ASN3 3.2 31.5 1.0 ND2 B:ASN37 3.4 22.6 1.0 CA B:THR104 3.5 24.9 1.0 N B:LEU6 3.6 23.4 1.0 CB B:THR104 3.7 24.5 1.0 OD1 B:ASN37 3.7 24.3 1.0 C B:THR104 3.8 26.2 1.0 CB B:GLU5 3.8 21.6 1.0 CB B:LEU6 3.9 22.9 1.0 CB B:SER39 3.9 29.9 1.0 CB B:ASN3 3.9 25.6 1.0 CG B:ASN37 4.0 30.9 1.0 CG B:ASN3 4.0 26.7 1.0 CA B:LEU6 4.1 24.1 1.0 C B:GLU5 4.1 23.7 1.0 CA B:GLY105 4.2 26.3 1.0 OG B:SER39 4.3 34.4 1.0 CA B:GLU5 4.5 22.8 1.0 CG2 B:THR104 4.5 24.5 1.0 O B:VAL103 4.6 25.7 1.0 OE1 B:GLU5 4.7 40.4 1.0 N B:THR104 4.8 24.9 1.0 N B:GLU5 4.8 25.3 1.0 O B:GLU5 4.8 25.9 1.0 O B:HOH463 4.9 57.4 1.0 OG1 B:THR104 4.9 26.0 1.0 CG B:GLU5 5.0 24.6 1.0 O B:THR104 5.0 26.8 1.0

D.Xia, L.Esser, S.K.Singh, F.Guo, M.R.Maurizi. Crystallographic Investigation of Peptide Binding Sites in the N-Domain of the Clpa Chaperone J.Struct.Biol. V. 146 166 2004.
ISSN: ISSN 1047-8477
PubMed: 15037248
DOI: 10.1016/J.JSB.2003.11.025