Chlorine in PDB 1oru: Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis

The structure of Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis, PDB code: 1oru was solved by Y.Kim, A.Joachimiak, A.Edwards, T.Skarina, A.Savchenko, Midwestcenter For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.07 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.652, 87.202, 122.249, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.5

The binding sites of Chlorine atom in the Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis (pdb code 1oru). 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 APC1665, Yuad Protein From Bacillus Subtilis, PDB code: 1oru:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis


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 APC1665, Yuad Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl504 b:59.1 occ:1.00 O A:HOH632 3.4 37.3 1.0 NH1 B:ARG166 3.8 25.0 1.0 O A:HOH604 3.9 38.7 1.0 NH2 B:ARG166 3.9 25.5 1.0 OG A:SER55 4.1 34.2 1.0 CZ B:ARG166 4.3 25.9 1.0 CB A:SER55 4.6 29.0 1.0 OG1 A:THR58 4.9 23.7 1.0 O A:HOH612 4.9 36.4 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis


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 APC1665, Yuad Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl506 b:28.7 occ:1.00 NE A:ARG158 3.0 16.3 1.0 NH2 A:ARG50 3.1 31.9 1.0 N A:CYS129 3.2 23.6 0.5 N A:CYS129 3.2 24.4 0.5 NH2 A:ARG158 3.2 17.4 1.0 SG A:CYS129 3.3 32.4 0.2 CG A:PRO132 3.4 27.1 1.0 CZ A:ARG158 3.6 18.3 1.0 CD A:PRO132 3.7 25.0 1.0 O A:ASP127 3.8 23.6 0.5 O A:ASP127 3.8 22.2 0.5 CA A:PRO128 3.8 23.5 1.0 CB A:CYS129 3.9 23.9 0.5 C A:PRO128 4.0 24.5 1.0 CB A:CYS129 4.0 27.5 0.5 CA A:CYS129 4.0 23.7 0.5 CA A:CYS129 4.1 25.7 0.5 CD A:ARG158 4.1 18.4 1.0 O A:CYS129 4.2 22.6 0.5 O A:CYS129 4.2 23.9 0.5 SG A:CYS129 4.4 25.0 0.5 CZ A:ARG50 4.4 30.7 1.0 CB A:PRO132 4.4 25.4 1.0 C A:CYS129 4.5 23.8 0.5 C A:CYS129 4.5 25.1 0.5 C A:ASP127 4.6 23.7 0.5 CE2 A:PHE150 4.7 25.1 1.0 C A:ASP127 4.7 21.9 0.5 N A:PRO128 4.7 22.6 1.0 CB A:PRO128 4.9 22.6 1.0 NH1 A:ARG158 4.9 17.7 1.0 ND2 A:ASN126 4.9 20.8 1.0 NH1 A:ARG50 5.0 29.6 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis


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 APC1665, Yuad Protein From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl505 b:22.0 occ:1.00 N B:CYS129 3.1 24.7 0.5 NE B:ARG158 3.1 15.1 1.0 N B:CYS129 3.1 24.4 0.5 NH2 B:ARG50 3.2 24.2 1.0 NH2 B:ARG158 3.3 14.5 1.0 SG B:CYS129 3.4 28.4 0.5 CG B:PRO132 3.4 21.3 1.0 CD B:PRO132 3.6 20.5 1.0 CZ B:ARG158 3.6 13.2 1.0 O B:ASP127 3.7 21.3 0.5 O B:ASP127 3.7 22.0 0.5 CA B:PRO128 3.8 23.6 1.0 CB B:CYS129 3.8 24.9 0.5 C B:PRO128 3.9 24.3 1.0 O B:HOH669 3.9 34.6 1.0 CB B:CYS129 3.9 26.2 0.5 CA B:CYS129 3.9 24.9 0.5 CA B:CYS129 3.9 25.6 0.5 CD B:ARG158 4.1 12.5 1.0 O B:CYS129 4.2 24.3 0.5 O B:CYS129 4.2 24.8 0.5 SG B:CYS129 4.3 25.6 0.5 C B:CYS129 4.4 25.0 0.5 C B:CYS129 4.4 25.4 0.5 CZ B:ARG50 4.5 23.5 1.0 CE2 B:PHE150 4.5 19.4 1.0 CB B:PRO132 4.6 19.7 1.0 C B:ASP127 4.6 22.4 0.5 C B:ASP127 4.6 23.0 0.5 O B:HOH543 4.6 26.7 1.0 N B:PRO128 4.7 22.8 1.0 CB B:PRO128 4.8 24.9 1.0 CZ B:PHE150 4.9 17.9 1.0 NH1 B:ARG50 4.9 22.6 1.0 NH1 B:ARG158 5.0 14.4 1.0

Y.Kim, A.Joachimiak, A.Edwards, T.Skarina, A.Savchenko. Crystal Structure of APC1665, Yuad Protein From Bacillus Subtilis To Be Published.