Chlorine in PDB 8xil: Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines

The structure of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8xil was solved by T.Kuga, N.Sunagawa, K.Igarashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.82 / 1.21
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	83.208, 88.778, 88.761, 98.58, 110.55, 110.56
R / Rfree (%)	14.3 / 16.4

The binding sites of Chlorine atom in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines (pdb code 8xil). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines, PDB code: 8xil:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1021 b:13.4 occ:1.00 HD22 A:ASN623 2.4 19.9 1.0 HE A:ARG717 2.4 14.2 1.0 HD21 A:ASN751 2.4 14.9 1.0 HH21 A:ARG717 2.6 15.6 1.0 HB2 A:ASN623 2.8 17.1 1.0 HB2 A:ASN751 2.9 14.8 1.0 HD2 A:PHE749 3.1 14.9 1.0 O A:HOH1534 3.1 13.2 1.0 NE A:ARG717 3.2 11.8 1.0 ND2 A:ASN623 3.2 16.6 1.0 HZ3 A:TRP622 3.2 16.4 1.0 ND2 A:ASN751 3.3 12.4 1.0 NH2 A:ARG717 3.3 13.0 1.0 HE3 A:TRP622 3.3 15.2 1.0 CB A:ASN623 3.7 14.2 1.0 HD12 A:LEU786 3.7 18.8 1.0 CZ A:ARG717 3.7 12.4 1.0 CB A:ASN751 3.7 12.4 1.0 HD21 A:ASN623 3.8 19.9 1.0 CZ3 A:TRP622 3.8 13.7 1.0 CE3 A:TRP622 3.8 12.6 1.0 HD22 A:ASN751 3.8 14.9 1.0 HB3 A:PHE749 3.9 14.2 1.0 CD2 A:PHE749 3.9 12.4 1.0 CG A:ASN623 3.9 15.3 1.0 HB3 A:ASN623 4.0 17.1 1.0 HB3 A:ASN751 4.0 14.8 1.0 CG A:ASN751 4.0 12.1 1.0 HH22 A:ARG717 4.0 15.6 1.0 H A:ASN751 4.2 12.2 1.0 HD3 A:ARG717 4.2 14.1 1.0 CD A:ARG717 4.3 11.7 1.0 HG A:LEU786 4.3 17.4 1.0 HE2 A:PHE749 4.4 15.7 1.0 HD22 A:LEU786 4.4 20.9 1.0 HD12 A:LEU626 4.5 20.0 1.0 SD A:MET666 4.5 12.1 1.0 CD1 A:LEU786 4.5 15.6 1.0 CE2 A:PHE749 4.6 13.1 1.0 HG2 A:ARG717 4.6 14.4 1.0 CB A:PHE749 4.7 11.8 1.0 HD11 A:LEU786 4.7 18.8 1.0 CG A:PHE749 4.8 11.5 1.0 CA A:ASN623 4.8 15.0 1.0 CG A:LEU786 4.9 14.5 1.0 N A:ASN751 4.9 10.1 1.0 H A:ASN623 4.9 15.6 1.0 CA A:ASN751 4.9 11.4 1.0 HA A:ASN623 5.0 18.0 1.0 CH2 A:TRP622 5.0 14.0 1.0

Chlorine binding site 2 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1022 b:12.2 occ:1.00 H A:LEU887 2.5 13.5 0.3 H A:LEU887 2.5 13.5 0.7 H A:THR491 2.5 12.7 1.0 H A:GLN490 2.7 12.3 1.0 HA3 A:GLY489 2.8 14.2 1.0 HD2 A:HIS140 3.0 13.5 1.0 HB2 A:LEU887 3.1 13.6 0.3 N A:GLN490 3.1 10.2 1.0 HA A:PRO886 3.1 12.9 1.0 HD11 A:LEU887 3.1 19.3 0.7 H A:GLN492 3.2 13.9 0.5 HE2 A:HIS140 3.2 13.9 0.0 N A:LEU887 3.3 11.3 0.3 HB2 A:PRO886 3.3 14.8 1.0 HB3 A:GLN490 3.3 13.8 1.0 N A:LEU887 3.3 11.2 0.7 HD11 A:LEU887 3.3 16.2 0.3 N A:THR491 3.3 10.6 1.0 HB3 A:PRO886 3.4 14.8 1.0 HB2 A:LEU887 3.4 14.6 0.7 HG A:LEU887 3.4 14.9 0.7 OG1 A:THR491 3.5 11.7 1.0 HG A:LEU887 3.6 15.4 0.3 CB A:PRO886 3.6 12.3 1.0 CD2 A:HIS140 3.6 11.2 1.0 CA A:GLY489 3.6 11.8 1.0 CA A:PRO886 3.7 10.7 1.0 C A:GLY489 3.7 12.2 1.0 NE2 A:HIS140 3.7 11.6 1.0 CB A:LEU887 3.8 11.3 0.3 CA A:GLN490 3.9 10.4 1.0 CD1 A:LEU887 3.9 16.1 0.7 CG A:LEU887 3.9 12.4 0.7 N A:GLN492 4.0 11.6 1.0 CB A:LEU887 4.0 12.2 0.7 CG A:LEU887 4.0 12.8 0.3 HG1 A:THR491 4.0 14.0 0.0 CB A:GLN490 4.0 11.5 1.0 C A:PRO886 4.0 11.1 1.0 CD1 A:LEU887 4.1 13.5 0.3 HA2 A:GLY489 4.1 14.2 1.0 C A:GLN490 4.1 10.6 1.0 CA A:LEU887 4.1 11.1 0.3 HB3 A:GLN492 4.2 18.8 0.5 CA A:LEU887 4.3 12.0 0.7 CA A:THR491 4.3 10.8 1.0 HD12 A:LEU887 4.3 19.3 0.7 HB2 A:GLN492 4.4 18.8 0.6 HB2 A:GLN490 4.4 13.8 1.0 H A:LEU888 4.4 18.4 0.7 CB A:THR491 4.5 11.1 1.0 H A:LEU888 4.5 15.3 0.3 C A:THR491 4.5 13.2 1.0 HD23 A:LEU888 4.6 24.5 0.3 HD12 A:LEU887 4.6 16.2 0.3 HB3 A:LEU887 4.6 13.6 0.3 HD13 A:LEU887 4.7 19.3 0.7 CB A:GLN492 4.7 15.7 1.0 O A:GLY489 4.7 16.0 1.0 N A:GLY489 4.7 11.8 1.0 HG23 A:THR491 4.7 12.8 1.0 HD13 A:LEU887 4.8 16.2 0.3 HA A:GLN490 4.8 12.5 1.0 HA A:LEU887 4.8 13.4 0.3 HD22 A:LEU888 4.9 24.5 0.3 HB3 A:LEU887 4.9 14.6 0.7 O A:PHE488 4.9 10.8 0.6 HA A:LEU887 4.9 14.4 0.7 CG A:HIS140 5.0 11.2 1.0 CA A:GLN492 5.0 13.0 1.0 HA3 A:GLY885 5.0 13.8 1.0

Chlorine binding site 3 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1020 b:46.4 occ:1.00 H B:LYS116 2.2 20.8 1.0 HG3 B:PRO51 2.9 32.3 1.0 NZ B:LYS116 2.9 39.7 1.0 HA B:ASP114 3.0 20.7 1.0 N B:LYS116 3.0 17.3 1.0 CG B:LYS116 3.1 30.9 1.0 H B:VAL115 3.1 21.1 1.0 CD B:LYS116 3.2 35.1 1.0 N B:VAL115 3.3 17.6 1.0 CE B:LYS116 3.5 38.4 1.0 CB B:LYS116 3.5 25.1 1.0 O B:SER113 3.5 23.1 1.0 C B:ASP114 3.6 16.7 1.0 HB B:VAL115 3.6 21.0 1.0 CA B:ASP114 3.7 17.3 1.0 CG B:PRO51 3.8 26.9 1.0 CA B:LYS116 3.8 19.8 1.0 HG2 B:PRO51 3.9 32.3 1.0 C B:VAL115 4.0 16.8 1.0 CA B:VAL115 4.0 16.5 1.0 C B:SER113 4.1 20.0 1.0 N B:ASP114 4.1 18.9 1.0 O B:VAL112 4.2 26.4 1.0 O B:ASP114 4.3 15.9 1.0 CB B:VAL115 4.3 17.5 1.0 O B:HOH1142 4.4 46.2 1.0 HA B:LYS116 4.5 23.7 1.0 HB3 B:PRO51 4.5 32.1 1.0 H B:HIS117 4.5 18.7 1.0 CB B:PRO51 4.5 26.8 1.0 HB2 B:PRO51 4.5 32.1 1.0 OD1 B:ASP114 4.6 19.8 1.0 H B:ASP114 4.7 22.7 1.0 HD3 B:PRO51 4.8 30.3 1.0 CD B:PRO51 4.9 25.2 1.0 C B:LYS116 4.9 16.9 1.0 O B:HOH1608 4.9 51.9 1.0 HA B:VAL115 4.9 19.8 1.0 HG23 B:VAL115 5.0 22.3 1.0

Chlorine binding site 4 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1021 b:13.8 occ:1.00 HE B:ARG717 2.4 15.0 1.0 HD22 B:ASN623 2.4 19.1 1.0 HD22 B:ASN751 2.4 14.8 1.0 HH21 B:ARG717 2.5 16.0 1.0 HB2 B:ASN623 2.8 16.4 1.0 HB2 B:ASN751 2.9 13.4 1.0 HD2 B:PHE749 3.1 15.4 1.0 O B:HOH1526 3.1 13.8 1.0 NE B:ARG717 3.2 12.5 1.0 HZ3 B:TRP622 3.2 15.7 1.0 ND2 B:ASN623 3.2 15.9 1.0 ND2 B:ASN751 3.3 12.3 1.0 NH2 B:ARG717 3.3 13.3 1.0 HE3 B:TRP622 3.3 15.5 1.0 CB B:ASN623 3.7 13.6 1.0 HD12 B:LEU786 3.7 18.2 1.0 CZ B:ARG717 3.7 12.7 1.0 CZ3 B:TRP622 3.8 13.0 1.0 CB B:ASN751 3.8 11.1 1.0 HD21 B:ASN623 3.8 19.1 1.0 CE3 B:TRP622 3.8 12.9 1.0 HD21 B:ASN751 3.8 14.8 1.0 HB3 B:PHE749 3.9 14.7 1.0 CD2 B:PHE749 3.9 12.8 1.0 CG B:ASN623 3.9 15.3 1.0 HH22 B:ARG717 4.0 16.0 1.0 HB3 B:ASN623 4.0 16.4 1.0 CG B:ASN751 4.0 11.4 1.0 HB3 B:ASN751 4.1 13.4 1.0 H B:ASN751 4.2 11.8 1.0 HD3 B:ARG717 4.3 14.7 1.0 CD B:ARG717 4.3 12.2 1.0 HG B:LEU786 4.3 16.6 1.0 HD22 B:LEU786 4.4 20.7 1.0 HE2 B:PHE749 4.4 15.6 1.0 CD1 B:LEU786 4.5 15.2 1.0 SD B:MET666 4.5 12.1 1.0 HD12 B:LEU626 4.5 19.4 1.0 CE2 B:PHE749 4.6 12.9 1.0 HG2 B:ARG717 4.6 13.5 1.0 HD11 B:LEU786 4.7 18.2 1.0 CB B:PHE749 4.7 12.2 1.0 CG B:PHE749 4.7 11.8 1.0 CA B:ASN623 4.8 13.8 1.0 CG B:LEU786 4.8 13.8 1.0 H B:ASN623 4.9 15.3 1.0 N B:ASN751 4.9 9.8 1.0 HA B:ASN623 4.9 16.6 1.0 CA B:ASN751 5.0 10.6 1.0 CH2 B:TRP622 5.0 14.3 1.0 HD11 B:LEU626 5.0 19.4 1.0

Chlorine binding site 5 out of 5 in the Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Cellodextrin Phosphorylase From Clostridium Thermocellum Mutant - All Cysteine Residues Were Substituted with Serines within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1022 b:12.8 occ:1.00 H B:LEU887 2.4 13.4 1.0 H B:THR491 2.5 12.4 1.0 H B:GLN490 2.6 12.2 1.0 HA3 B:GLY489 2.9 15.8 1.0 HD2 B:HIS140 3.1 14.2 1.0 N B:GLN490 3.1 10.1 1.0 HA B:PRO886 3.2 12.8 1.0 HD11 B:LEU887 3.2 18.5 1.0 O B:HOH1745 3.2 18.1 1.0 HG2 B:GLN492 3.2 21.5 0.3 HB2 B:PRO886 3.2 14.6 1.0 H B:GLN492 3.2 15.3 0.3 H B:GLN492 3.2 13.4 0.7 N B:LEU887 3.3 11.1 1.0 HE2 B:HIS140 3.3 13.8 0.0 HB3 B:GLN490 3.3 13.7 1.0 HB2 B:LEU887 3.3 14.2 1.0 N B:THR491 3.4 10.3 1.0 HB3 B:PRO886 3.4 14.6 1.0 HG B:LEU887 3.4 14.7 1.0 OG1 B:THR491 3.5 11.4 1.0 CB B:PRO886 3.6 12.2 1.0 CD2 B:HIS140 3.7 11.8 1.0 CA B:GLY489 3.7 13.2 1.0 CA B:PRO886 3.7 10.6 1.0 C B:GLY489 3.7 13.1 1.0 NE2 B:HIS140 3.8 11.4 1.0 CA B:GLN490 3.9 10.6 1.0 CG B:LEU887 3.9 12.2 1.0 CB B:LEU887 3.9 11.8 1.0 HG3 B:GLN492 3.9 21.5 0.3 CD1 B:LEU887 3.9 15.4 1.0 CG B:GLN492 4.0 17.9 0.3 N B:GLN492 4.0 12.7 0.3 N B:GLN492 4.0 11.2 0.7 C B:PRO886 4.0 11.4 1.0 HG1 B:THR491 4.0 13.8 0.0 CB B:GLN490 4.0 11.4 1.0 C B:GLN490 4.1 10.9 1.0 HA2 B:GLY489 4.2 15.8 1.0 HB3 B:GLN492 4.2 17.2 0.7 CA B:LEU887 4.2 12.4 1.0 CA B:THR491 4.3 11.1 1.0 H B:LEU888 4.3 18.7 1.0 HB2 B:GLN492 4.3 17.2 0.7 HB2 B:GLN492 4.3 19.5 0.3 HD12 B:LEU887 4.4 18.5 1.0 HB2 B:GLN490 4.4 13.7 1.0 CB B:THR491 4.5 11.4 1.0 C B:THR491 4.6 12.9 1.0 CB B:GLN492 4.6 16.2 0.3 CB B:GLN492 4.6 14.3 0.7 HD13 B:LEU887 4.7 18.5 1.0 N B:GLY489 4.7 12.0 1.0 O B:GLY489 4.7 15.6 1.0 HG23 B:THR491 4.8 13.6 1.0 HA B:GLN490 4.8 12.8 1.0 HB3 B:LEU887 4.8 14.2 1.0 HA B:LEU887 4.9 14.9 1.0 O B:PHE488 4.9 17.5 1.0 CA B:GLN492 4.9 13.9 0.3 CA B:GLN492 5.0 12.4 0.7 CG B:HIS140 5.0 10.9 1.0 HA3 B:GLY885 5.0 14.0 1.0

T.Kuga, N.Sunagawa, K.Igarashi. Effect of Free Cysteine Residues to Serine Mutation on Cellodextrin Phosphorylase To Be Published.