Chlorine in PDB 7toj: Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme

The structure of Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme, PDB code: 7toj was solved by P.J.Stogios, T.Skarina, R.Di Leo, E.Jurak, E.Master, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.36 / 1.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.16, 77.31, 42.08, 90, 96.89, 90
R / Rfree (%)	14.1 / 16.4

The binding sites of Chlorine atom in the Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme (pdb code 7toj). 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 Carbohydrate Esterase Cspacxe, Apoenzyme, PDB code: 7toj:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme


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 Carbohydrate Esterase Cspacxe, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:22.7 occ:0.92 N A:GLY230 3.1 22.9 1.0 OG A:SER189 3.2 24.6 1.0 ND2 A:ASN266 3.2 21.1 1.0 N A:SER189 3.2 18.4 1.0 CB A:SER189 3.3 22.1 1.0 CB A:ASN188 3.6 18.4 1.0 CA A:GLY230 3.7 24.4 1.0 CG A:ASN188 3.8 20.7 1.0 CA A:SER189 3.9 18.2 1.0 OD1 A:ASN266 4.0 26.5 1.0 CG A:ASN266 4.1 21.4 1.0 O A:HOH920 4.2 47.7 1.0 C A:GLY229 4.2 23.1 1.0 ND2 A:ASN188 4.2 22.3 1.0 OD1 A:ASN188 4.2 20.6 1.0 C A:ASN188 4.3 16.9 1.0 CA A:GLY229 4.4 21.8 1.0 C A:GLY230 4.5 22.2 1.0 CA A:ASN188 4.5 16.3 1.0 N A:ASN231 4.6 19.7 1.0 C A:SER189 4.8 17.5 1.0 N A:ILE190 4.9 18.0 1.0 O A:ILE228 5.0 17.6 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme


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 Carbohydrate Esterase Cspacxe, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:18.9 occ:0.52 O A:HOH924 2.7 18.6 1.0 N A:ASN225 3.0 14.6 1.0 O A:VAL223 3.0 16.9 1.0 N A:ALA18 3.1 14.2 1.0 O A:ALA18 3.2 15.0 1.0 CA A:LEU224 3.3 14.2 1.0 O A:HOH711 3.5 20.0 1.0 C A:LEU224 3.6 13.9 1.0 CA A:TRP17 3.6 13.9 1.0 CD1 A:TRP17 3.8 15.7 1.0 C A:TRP17 3.8 13.9 1.0 C A:VAL223 3.9 15.3 1.0 CB A:ASN225 3.9 15.9 1.0 C A:ALA18 4.0 14.2 1.0 CA A:ASN225 4.0 15.1 1.0 N A:LEU224 4.0 15.2 1.0 CA A:ALA18 4.1 14.2 1.0 O A:HOH613 4.1 17.8 1.0 CG A:TRP17 4.2 14.3 1.0 O A:HOH679 4.2 22.4 0.6 O A:HOH679 4.3 30.1 0.4 NE1 A:TRP17 4.3 15.8 1.0 CD2 A:LEU224 4.4 17.3 1.0 CB A:TRP17 4.4 15.0 1.0 CB A:LEU224 4.4 15.9 1.0 CB A:ALA18 4.6 15.9 1.0 O A:HOH563 4.7 19.0 1.0 O A:THR16 4.7 14.9 1.0 N A:TRP17 4.7 14.1 1.0 O A:HOH785 4.8 19.6 1.0 O A:ASN225 4.8 15.6 1.0 O A:LEU224 4.8 15.0 1.0 C A:ASN225 4.9 15.1 1.0 CD2 A:TRP17 4.9 14.3 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Carbohydrate Esterase Cspacxe, Apoenzyme


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 Carbohydrate Esterase Cspacxe, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:20.5 occ:0.54 OG A:SER144 2.8 18.0 1.0 O A:THR143 2.9 19.4 1.0 N A:ILE43 2.9 16.3 1.0 NE1 A:TRP166 3.1 16.4 1.0 C A:THR143 3.4 18.4 1.0 CA A:GLN42 3.4 16.8 1.0 CG2 A:THR142 3.4 17.9 1.0 CD1 A:TRP166 3.5 16.7 1.0 C A:GLN42 3.6 16.2 1.0 N A:SER144 3.6 19.1 1.0 O A:ILE43 3.6 16.7 1.0 CA A:SER144 3.7 19.6 1.0 CB A:SER144 3.8 17.6 1.0 CB A:GLN42 3.8 17.0 1.0 O A:THR142 3.9 19.7 1.0 CA A:ILE43 3.9 16.9 1.0 CB A:THR142 3.9 17.5 1.0 C A:THR142 4.1 18.9 1.0 CB A:ILE43 4.1 18.0 1.0 C A:ILE43 4.2 16.1 1.0 CG1 A:ILE43 4.3 22.3 1.0 CE2 A:TRP166 4.3 15.0 1.0 N A:THR143 4.4 18.8 1.0 CG A:GLN42 4.4 17.5 1.0 CA A:THR143 4.5 19.1 1.0 O A:ARG41 4.5 19.1 1.0 N A:GLN42 4.6 16.4 1.0 CA A:THR142 4.7 17.7 1.0 O A:HOH636 4.7 21.8 1.0 O A:GLN42 4.8 18.0 1.0 CG A:TRP166 4.8 16.4 1.0 O A:HIS165 4.9 19.1 1.0

L.Penttinen, V.Kouhi, R.Faure, T.Skarina, P.Stogios, E.Master, E.Jurak. Elucidating Sequence and Structural Determinants of Carbohydrate Esterases For Complete Deacetylation of Substituted Xylans. Molecules V. 27 2022.
ISSN: ESSN 1420-3049
PubMed: 35566004
DOI: 10.3390/MOLECULES27092655