Chlorine in PDB 6lcn: Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A

All present enzymatic activity of Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A:
2.3.1.30;

The structure of Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A, PDB code: 6lcn was solved by N.Kumar, R.P.Singh, A.K.Singh, S.Kumaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.60 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.719, 113.165, 230.133, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 22.3

The binding sites of Chlorine atom in the Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A (pdb code 6lcn). 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 Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A, PDB code: 6lcn:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A


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 Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:82.9 occ:1.00 O A:HOH571 2.9 45.7 1.0 O A:ILE216 2.9 31.4 1.0 O A:ASP195 3.2 30.2 1.0 OD1 A:ASP195 3.3 36.3 1.0 CE1 E:HIS210 3.5 36.9 1.0 N A:HIS197 3.5 29.8 1.0 C A:ILE216 3.6 30.8 1.0 CG1 A:VAL215 3.6 25.5 1.0 CG A:ASP195 3.7 32.2 1.0 ND1 E:HIS210 3.8 32.9 1.0 N A:ILE216 3.8 29.8 1.0 C A:ASP195 3.9 32.7 1.0 O A:HOH607 4.0 40.4 1.0 CB A:HIS197 4.0 25.6 1.0 OD2 A:ASP195 4.0 31.6 1.0 C A:ILE196 4.1 31.4 1.0 CA A:HIS197 4.2 28.3 1.0 N A:GLY217 4.3 29.1 1.0 CA A:GLY217 4.3 27.8 1.0 CA A:ILE196 4.4 28.7 1.0 CA A:ILE216 4.4 29.0 1.0 N A:ILE196 4.4 30.8 1.0 CB A:ASP195 4.4 30.9 1.0 C A:VAL215 4.6 31.8 1.0 NE2 E:HIS210 4.6 38.6 1.0 CA A:VAL215 4.7 27.6 1.0 O A:HOH583 4.7 36.2 1.0 CB A:VAL215 4.8 27.6 1.0 CA A:ASP195 4.8 29.9 1.0 O A:HOH573 4.8 24.7 1.0 O A:ILE196 5.0 34.2 1.0 CG A:HIS197 5.0 26.9 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A


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 Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl603 b:65.7 occ:1.00 OG1 C:THR185 2.9 23.9 1.0 O C:ILE196 3.0 18.9 1.0 OD1 C:ASP195 3.2 27.4 1.0 OE2 C:GLU186 3.2 28.5 1.0 O C:HOH790 3.2 43.1 1.0 CB C:THR185 3.4 24.6 1.0 CD C:GLU186 3.5 25.7 1.0 NE C:ARG182 3.6 26.4 1.0 C C:ILE196 3.6 20.4 1.0 C C:THR185 3.8 24.9 1.0 CD C:ARG182 3.9 25.2 1.0 N C:GLU186 4.0 22.3 1.0 N C:ILE196 4.0 22.1 1.0 O C:THR185 4.0 24.7 1.0 CG C:GLU186 4.0 24.6 1.0 OE1 C:GLU186 4.0 25.4 1.0 N C:HIS197 4.1 21.8 1.0 O C:HOH761 4.1 19.5 1.0 CA C:HIS197 4.2 24.0 1.0 CA C:THR185 4.2 25.1 1.0 CG C:ASP195 4.4 26.3 1.0 CA C:GLU186 4.4 22.9 1.0 C C:ASP195 4.5 22.6 1.0 CA C:ILE196 4.5 21.5 1.0 CZ C:ARG182 4.5 27.9 1.0 CD C:PRO198 4.5 24.9 1.0 CG2 C:THR185 4.6 23.0 1.0 O C:HOH730 4.7 23.4 1.0 CA C:ASP195 4.7 22.1 1.0 O C:HOH792 4.8 34.0 1.0 NH2 C:ARG182 4.8 25.6 1.0 CB C:GLU186 4.9 24.2 1.0 CB C:HIS189 4.9 22.2 1.0 O C:ARG182 5.0 23.9 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A


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 Serine Acetyltransferase From Planctomyces Limnophilus at 2.15A within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl403 b:54.4 occ:1.00 O D:HOH569 2.8 28.0 1.0 C D:GLY159 3.0 22.0 1.0 N D:ILE208 3.0 24.9 1.0 O D:GLY159 3.1 26.1 1.0 N D:LEU160 3.4 21.8 1.0 CA D:GLY159 3.5 20.3 1.0 CA D:PHE207 3.5 27.3 1.0 CD1 D:PHE207 3.7 29.8 1.0 C D:PHE207 3.8 27.2 1.0 CG2 D:VAL163 3.8 25.4 1.0 CA D:LEU160 3.8 22.5 1.0 O D:ILE208 3.9 24.4 1.0 O D:PHE206 4.0 25.9 1.0 CA D:ILE208 4.0 23.5 1.0 CB D:ILE208 4.2 23.3 1.0 C D:ILE208 4.4 24.3 1.0 CB D:PHE207 4.4 27.6 1.0 N D:PHE207 4.4 27.8 1.0 CB D:VAL163 4.5 25.4 1.0 CE1 D:PHE207 4.5 28.8 1.0 CG D:PHE207 4.5 30.5 1.0 C D:PHE206 4.6 26.9 1.0 CB D:LEU160 4.7 22.3 1.0 N D:GLY159 4.7 21.6 1.0 CG1 D:ILE208 4.8 19.8 1.0 O D:PHE207 5.0 29.2 1.0 C D:LEU160 5.0 24.3 1.0

N.Kumar, R.P.Singh, S.Kumaran. Understanding Mechanics of Competitive-Allostery Using Engineered Cysteine Synthase Assembly To Be Published.