Chlorine in PDB 7l8n: Diadenylate Cyclase with Amp From Streptococcus Mutans

All present enzymatic activity of Diadenylate Cyclase with Amp From Streptococcus Mutans:
2.7.7.85;

The structure of Diadenylate Cyclase with Amp From Streptococcus Mutans, PDB code: 7l8n was solved by Z.Hua, W.Hui, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.97 / 1.94
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	76.36, 84.59, 100.24, 90, 90, 90
R / Rfree (%)	16.1 / 20.7

The binding sites of Chlorine atom in the Diadenylate Cyclase with Amp From Streptococcus Mutans (pdb code 7l8n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Diadenylate Cyclase with Amp From Streptococcus Mutans, PDB code: 7l8n:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Diadenylate Cyclase with Amp From Streptococcus Mutans


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Diadenylate Cyclase with Amp From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:43.4 occ:1.00 H B:SER251 2.8 37.0 1.0 HA B:LEU250 2.8 36.2 1.0 O B:HOH408 3.2 35.3 1.0 N B:SER251 3.5 30.8 1.0 HD23 B:LEU250 3.6 42.3 1.0 CA B:LEU250 3.7 30.1 1.0 HB3 B:ALA254 3.8 35.2 1.0 HB2 B:ALA254 3.8 35.2 1.0 O B:ASP249 3.9 33.2 1.0 HB3 B:SER251 4.0 32.9 1.0 HB1 B:ALA254 4.1 35.2 1.0 CB B:ALA254 4.1 29.3 1.0 C B:LEU250 4.1 33.9 1.0 HB3 B:LEU250 4.5 32.7 1.0 CD2 B:LEU250 4.5 35.2 1.0 CB B:LEU250 4.6 27.2 1.0 N B:LEU250 4.6 27.9 1.0 CB B:SER251 4.6 27.3 1.0 OG B:SER251 4.6 25.7 1.0 C B:ASP249 4.6 37.1 1.0 CA B:SER251 4.7 31.5 1.0 HD22 B:LEU250 4.8 42.3 1.0 HG B:LEU250 5.0 31.9 1.0 CG B:LEU250 5.0 26.5 1.0

Chlorine binding site 2 out of 2 in the Diadenylate Cyclase with Amp From Streptococcus Mutans


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Diadenylate Cyclase with Amp From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:46.5 occ:1.00 HE2 B:HIS214 1.9 38.3 1.0 HG B:SER239 2.4 40.5 1.0 NE2 B:HIS214 2.7 31.8 1.0 OG B:SER239 2.7 33.7 1.0 O B:ALA237 2.8 22.0 1.0 HB2 B:SER239 2.9 32.0 1.0 HB2 B:SER232 3.1 30.3 1.0 CB B:SER239 3.3 26.6 1.0 HB3 B:ALA237 3.3 31.5 1.0 H B:SER232 3.4 29.1 1.0 C B:ALA237 3.4 23.6 1.0 CD2 B:HIS214 3.5 37.5 1.0 H B:SER239 3.5 26.0 1.0 HD2 B:HIS214 3.5 45.1 1.0 HD2 B:HIS248 3.5 63.8 1.0 N B:SER239 3.6 21.6 1.0 HB B:VAL230 3.7 29.9 1.0 HG12 B:VAL230 3.7 29.9 1.0 HB1 B:ALA237 3.7 31.5 1.0 CE1 B:HIS214 3.7 37.0 1.0 CB B:SER232 3.8 25.2 1.0 N B:SER232 3.8 24.2 1.0 HB3 B:SER232 3.9 30.3 1.0 C B:ILE238 3.9 26.5 1.0 CB B:ALA237 3.9 26.2 1.0 O B:VAL230 3.9 21.7 1.0 HA B:ILE238 3.9 27.4 1.0 HE1 B:HIS214 3.9 44.5 1.0 N B:ILE238 4.1 22.5 1.0 CA B:SER239 4.1 22.7 1.0 HA B:VAL231 4.1 21.4 1.0 HB3 B:SER239 4.1 32.0 1.0 CA B:ILE238 4.2 22.8 1.0 CD2 B:HIS248 4.2 53.2 1.0 CA B:ALA237 4.2 26.3 1.0 CG1 B:VAL230 4.3 24.9 1.0 CA B:SER232 4.3 21.8 1.0 HZ B:PHE246 4.4 39.4 1.0 HE1 B:PHE210 4.4 76.2 1.0 H B:ASP249 4.4 34.9 1.0 C B:VAL230 4.4 21.4 1.0 HG11 B:VAL230 4.4 29.9 1.0 CB B:VAL230 4.4 24.9 1.0 O B:ILE238 4.5 23.4 1.0 HA B:SER232 4.5 26.2 1.0 NE2 B:HIS248 4.5 59.7 1.0 C B:VAL231 4.5 20.3 1.0 HA B:SER239 4.6 27.3 1.0 CA B:VAL231 4.6 17.8 1.0 H B:ILE238 4.7 27.1 1.0 CG B:HIS214 4.7 37.4 1.0 HB2 B:ALA237 4.8 31.5 1.0 ND1 B:HIS214 4.8 41.9 1.0 N B:VAL231 4.8 17.1 1.0 N B:ALA237 4.9 23.3 1.0 H B:ALA237 4.9 28.1 1.0

Z.Hua, W.Hui. Diadenylate Cyclase with Amp From Streptococcus Mutans To Be Published.