Chlorine in PDB 8xis: 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: 8xis 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)	43.44 / 1.68
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	82.277, 88.52, 88.54, 98.41, 110.69, 110.65
R / Rfree (%)	18.8 / 23

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

Chlorine binding site 1 out of 4 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:Cl1013 b:18.6 occ:1.00 H A:LEU887 2.4 25.6 1.0 H A:THR491 2.5 19.2 1.0 H A:GLN490 2.7 22.8 1.0 HA3 A:GLY489 2.9 22.6 1.0 HB2 A:LEU887 3.1 18.9 1.0 HD2 A:HIS140 3.1 19.0 1.0 H A:GLN492 3.1 24.0 1.0 HG2 A:GLN492 3.1 37.5 1.0 N A:GLN490 3.1 19.0 1.0 HB3 A:PRO886 3.2 24.1 1.0 N A:LEU887 3.2 21.3 1.0 HD11 A:LEU887 3.2 34.6 1.0 HA A:PRO886 3.2 22.1 1.0 HB3 A:GLN490 3.3 19.4 1.0 N A:THR491 3.3 16.0 1.0 HB2 A:PRO886 3.4 24.1 1.0 HE2 A:HIS140 3.4 17.4 0.0 OG1 A:THR491 3.5 16.7 1.0 CB A:PRO886 3.6 20.1 1.0 HG A:LEU887 3.7 25.6 1.0 CA A:GLY489 3.7 18.9 1.0 CA A:PRO886 3.7 18.4 1.0 C A:GLY489 3.7 18.3 1.0 CD2 A:HIS140 3.7 15.8 1.0 CB A:LEU887 3.8 15.7 1.0 NE2 A:HIS140 3.9 14.5 1.0 N A:GLN492 3.9 20.0 1.0 CA A:GLN490 3.9 14.7 1.0 HD21 A:LEU888 4.0 50.3 1.0 CG A:GLN492 4.0 31.2 1.0 C A:PRO886 4.0 22.9 1.0 CB A:GLN490 4.0 16.1 1.0 CG A:LEU887 4.0 21.3 1.0 CD1 A:LEU887 4.0 28.8 1.0 HG1 A:THR491 4.1 20.0 0.0 HG3 A:GLN492 4.1 37.5 1.0 CA A:LEU887 4.1 20.2 1.0 C A:GLN490 4.1 17.6 1.0 CA A:THR491 4.2 17.0 1.0 HB2 A:GLN492 4.3 29.3 1.0 H A:LEU888 4.3 28.0 1.0 HA2 A:GLY489 4.3 22.6 1.0 HD23 A:LEU888 4.4 50.3 1.0 HB2 A:GLN490 4.4 19.4 1.0 CB A:THR491 4.5 14.8 1.0 C A:THR491 4.5 20.3 1.0 HD12 A:LEU887 4.5 34.6 1.0 CD2 A:LEU888 4.5 41.9 1.0 N A:GLY489 4.6 18.8 1.0 CB A:GLN492 4.6 24.4 1.0 HB3 A:LEU887 4.6 18.9 1.0 HD22 A:LEU888 4.6 50.3 1.0 H A:GLY489 4.7 22.6 1.0 O A:GLY489 4.7 19.1 1.0 HD13 A:LEU887 4.7 34.6 1.0 HG23 A:THR491 4.8 17.9 1.0 HA A:GLN490 4.8 17.7 1.0 HA A:LEU887 4.9 24.2 1.0 CA A:GLN492 4.9 19.4 1.0 N A:LEU888 4.9 23.3 1.0 C A:LEU887 5.0 25.6 1.0

Chlorine binding site 2 out of 4 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:Cl1014 b:27.1 occ:1.00 HH11 A:ARG717 2.0 35.6 0.2 NH1 A:ARG717 2.3 29.7 0.2 HE A:ARG717 2.4 27.9 0.8 HH12 A:ARG717 2.5 35.6 0.2 HD22 A:ASN751 2.5 39.5 1.0 HD21 A:ASN623 2.6 46.2 1.0 HB2 A:ASN751 2.6 32.8 1.0 HH21 A:ARG717 2.7 36.4 0.8 HB2 A:ASN623 2.8 41.8 1.0 O A:HOH1371 3.0 28.1 1.0 HD2 A:PHE749 3.2 43.8 1.0 CZ A:ARG717 3.2 32.6 0.2 NE A:ARG717 3.2 23.2 0.8 ND2 A:ASN751 3.3 32.9 1.0 ND2 A:ASN623 3.4 38.5 1.0 NH2 A:ARG717 3.4 30.3 0.8 HE3 A:TRP622 3.4 38.4 1.0 CB A:ASN751 3.5 27.3 1.0 HZ3 A:TRP622 3.5 28.3 1.0 HH22 A:ARG717 3.5 40.3 0.2 HB3 A:ASN751 3.6 32.8 1.0 CB A:ASN623 3.7 34.8 1.0 NH2 A:ARG717 3.7 33.6 0.2 CZ A:ARG717 3.8 32.8 0.8 HB3 A:PHE749 3.8 36.4 1.0 HD12 A:LEU786 3.9 34.4 1.0 CG A:ASN751 3.9 31.5 1.0 HD3 A:ARG717 3.9 35.3 0.2 CD2 A:PHE749 3.9 36.5 1.0 HD21 A:ASN751 4.0 39.5 1.0 CE3 A:TRP622 4.0 31.9 1.0 HD22 A:ASN623 4.0 46.2 1.0 CG A:ASN623 4.0 45.8 1.0 CZ3 A:TRP622 4.0 23.6 1.0 HB3 A:ASN623 4.0 41.8 1.0 H A:ASN751 4.1 32.5 1.0 NE A:ARG717 4.1 32.9 0.2 HH22 A:ARG717 4.1 36.4 0.8 HD3 A:ARG717 4.2 29.6 0.8 CD A:ARG717 4.3 24.6 0.8 HG3 A:ARG717 4.4 42.9 0.2 SD A:MET666 4.4 27.0 1.0 HH21 A:ARG717 4.5 40.3 0.2 CD A:ARG717 4.5 29.4 0.2 HD12 A:LEU626 4.5 41.5 1.0 HD11 A:LEU786 4.5 34.4 1.0 HE2 A:PHE749 4.5 41.9 1.0 HD22 A:LEU786 4.6 39.4 1.0 CD1 A:LEU786 4.6 28.6 1.0 HG A:LEU786 4.6 39.5 1.0 CE2 A:PHE749 4.7 34.9 1.0 CB A:PHE749 4.7 30.3 1.0 CA A:ASN751 4.7 27.3 1.0 HG2 A:ARG717 4.7 34.6 0.8 HA A:ASN623 4.7 47.4 1.0 CG A:PHE749 4.8 36.2 1.0 CA A:ASN623 4.8 39.5 1.0 N A:ASN751 4.8 27.1 1.0 HE A:ARG717 4.8 39.5 0.2 CG A:ARG717 5.0 35.7 0.2 H A:ASN623 5.0 46.6 1.0

Chlorine binding site 3 out of 4 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:Cl1015 b:17.7 occ:1.00 H B:LEU887 2.3 26.4 1.0 H B:THR491 2.5 19.8 1.0 H B:GLN490 2.6 19.7 1.0 HA3 B:GLY489 2.9 22.8 1.0 HD2 B:HIS140 3.1 18.7 1.0 N B:GLN490 3.1 16.4 1.0 H B:GLN492 3.1 23.3 1.0 HB2 B:LEU887 3.1 19.5 1.0 HG2 B:GLN492 3.1 34.9 1.0 HA B:PRO886 3.2 22.6 1.0 N B:LEU887 3.2 21.9 1.0 HB2 B:PRO886 3.2 24.2 1.0 HB3 B:PRO886 3.2 24.2 1.0 HD11 B:LEU887 3.3 37.4 1.0 HB3 B:GLN490 3.3 21.8 1.0 N B:THR491 3.3 16.4 1.0 HE2 B:HIS140 3.5 19.0 0.0 CB B:PRO886 3.5 20.1 1.0 OG1 B:THR491 3.5 15.3 1.0 CA B:PRO886 3.6 18.8 1.0 C B:GLY489 3.7 17.6 1.0 CA B:GLY489 3.7 19.0 1.0 CD2 B:HIS140 3.7 15.6 1.0 HG B:LEU887 3.8 25.4 1.0 HD21 B:LEU888 3.8 57.8 1.0 CB B:LEU887 3.8 16.2 1.0 N B:GLN492 3.9 19.4 1.0 CA B:GLN490 3.9 17.9 1.0 NE2 B:HIS140 3.9 15.8 1.0 C B:PRO886 3.9 22.9 1.0 CG B:GLN492 4.0 29.0 1.0 CB B:GLN490 4.0 18.1 1.0 HG3 B:GLN492 4.0 34.9 1.0 HG1 B:THR491 4.1 18.4 0.0 CA B:LEU887 4.1 21.9 1.0 CD1 B:LEU887 4.1 31.1 1.0 CG B:LEU887 4.1 21.1 1.0 C B:GLN490 4.1 17.4 1.0 HD23 B:LEU888 4.2 57.8 1.0 HB2 B:GLN492 4.2 29.1 1.0 CA B:THR491 4.3 15.4 1.0 H B:LEU888 4.3 28.8 1.0 HA2 B:GLY489 4.3 22.8 1.0 CD2 B:LEU888 4.4 48.1 1.0 HB2 B:GLN490 4.4 21.8 1.0 CB B:THR491 4.5 17.5 1.0 HD22 B:LEU888 4.5 57.8 1.0 C B:THR491 4.5 20.4 1.0 CB B:GLN492 4.5 24.2 1.0 N B:GLY489 4.6 20.3 1.0 H B:GLY489 4.6 24.4 1.0 HD13 B:LEU887 4.6 37.4 1.0 O B:GLY489 4.7 18.8 1.0 HB3 B:LEU887 4.7 19.5 1.0 HD12 B:LEU887 4.7 37.4 1.0 HA B:GLN490 4.8 21.5 1.0 HG23 B:THR491 4.8 21.8 1.0 N B:LEU888 4.8 24.0 1.0 HA B:LEU887 4.8 26.3 1.0 CA B:GLN492 4.9 19.3 1.0 C B:LEU887 4.9 24.2 1.0

Chlorine binding site 4 out of 4 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:Cl1016 b:27.2 occ:1.00 HE B:ARG717 2.4 35.5 1.0 HD21 B:ASN751 2.5 41.9 1.0 HE3 B:MET666 2.5 17.6 0.4 HD21 B:ASN623 2.5 52.4 1.0 HH21 B:ARG717 2.6 44.4 1.0 HB2 B:ASN751 2.7 34.1 1.0 HB2 B:ASN623 2.8 40.2 1.0 O B:HOH1356 3.0 28.4 1.0 HE1 B:MET666 3.1 17.6 0.4 HD2 B:PHE749 3.1 41.6 1.0 CE B:MET666 3.2 14.6 0.4 NE B:ARG717 3.2 29.6 1.0 ND2 B:ASN751 3.3 34.9 1.0 ND2 B:ASN623 3.3 43.6 1.0 NH2 B:ARG717 3.4 37.0 1.0 HE3 B:TRP622 3.4 42.9 1.0 HE2 B:MET666 3.5 17.6 0.4 CB B:ASN751 3.5 28.4 1.0 HZ3 B:TRP622 3.5 27.9 1.0 HB3 B:ASN751 3.7 34.1 1.0 CB B:ASN623 3.7 33.5 1.0 HD12 B:LEU786 3.7 34.8 1.0 CZ B:ARG717 3.8 36.1 1.0 HB3 B:PHE749 3.8 34.1 1.0 HD22 B:ASN623 3.9 52.4 1.0 CG B:ASN751 3.9 32.1 1.0 CD2 B:PHE749 3.9 34.6 1.0 HD22 B:ASN751 3.9 41.9 1.0 CG B:ASN623 4.0 48.8 1.0 CE3 B:TRP622 4.0 35.7 1.0 HG3 B:MET666 4.0 42.2 0.4 CZ3 B:TRP622 4.0 23.2 1.0 HH22 B:ARG717 4.1 44.4 1.0 H B:ASN751 4.1 29.6 1.0 HB3 B:ASN623 4.1 40.2 1.0 HD3 B:ARG717 4.2 36.4 1.0 CD B:ARG717 4.4 30.3 1.0 SD B:MET666 4.4 24.4 0.6 HD12 B:LEU626 4.4 51.8 1.0 HD22 B:LEU786 4.4 34.9 1.0 HE2 B:PHE749 4.5 44.0 1.0 CD1 B:LEU786 4.5 29.0 1.0 HD11 B:LEU786 4.5 34.8 1.0 HG B:LEU786 4.6 39.5 1.0 CE2 B:PHE749 4.6 36.6 1.0 CB B:PHE749 4.7 28.4 1.0 HA B:ASN623 4.7 49.9 1.0 CA B:ASN751 4.7 24.8 1.0 CG B:PHE749 4.7 33.3 1.0 SD B:MET666 4.7 26.1 0.4 CA B:ASN623 4.8 41.6 1.0 HG2 B:ARG717 4.8 42.9 1.0 N B:ASN751 4.8 24.7 1.0 CG B:MET666 4.8 35.1 0.4 HD11 B:LEU626 4.9 51.8 1.0 CG B:LEU786 5.0 32.9 1.0

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