Chlorine in PDB 2yjq: Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44

All present enzymatic activity of Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44:
3.2.1.151; 3.2.1.4;

The structure of Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44, PDB code: 2yjq was solved by A.Ariza, J.M.Eklof, O.Spadiut, W.A.Offen, S.M.Roberts, W.Besenmatter, E.P.Friis, M.Skjot, K.S.Wilson, H.Brumer, G.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	106.68 / 2.25
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.200, 84.200, 320.050, 90.00, 90.00, 120.00
R / Rfree (%)	19.675 / 25.948

The structure of Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44 also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Chlorine atom in the Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44 (pdb code 2yjq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44, PDB code: 2yjq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1527 b:18.2 occ:1.00 N A:TYR234 3.1 19.6 1.0 N A:ALA189 3.1 18.5 1.0 C A:GLU187 3.3 18.4 1.0 CA A:GLU187 3.3 17.7 1.0 CB A:ALA189 3.4 17.3 1.0 CD A:PRO188 3.5 18.4 1.0 N A:PRO188 3.6 18.4 1.0 CA A:LEU233 3.6 20.1 1.0 CB A:ALA238 3.6 20.8 1.0 CA A:ALA189 3.7 18.5 1.0 CD1 A:TYR234 3.7 19.2 1.0 CB A:GLU187 3.7 18.1 1.0 O A:GLU187 3.7 19.9 1.0 C A:LEU233 3.8 20.7 1.0 N A:LEU190 4.0 17.3 1.0 CB A:TYR234 4.0 19.6 1.0 CD2 A:LEU233 4.1 20.0 1.0 O A:VAL232 4.1 18.0 1.0 CG A:PRO188 4.1 18.3 1.0 CA A:TYR234 4.1 19.8 1.0 C A:PRO188 4.1 18.6 1.0 C A:ALA189 4.2 18.6 1.0 CG A:TYR234 4.4 18.8 1.0 CA A:PRO188 4.4 19.0 1.0 CB A:LEU233 4.4 19.8 1.0 N A:LEU233 4.6 19.8 1.0 CG A:GLU187 4.6 19.1 1.0 N A:GLU187 4.6 16.6 1.0 CE1 A:TYR234 4.7 18.6 1.0 C A:VAL232 4.8 18.8 1.0 CG A:LEU233 4.9 21.2 1.0 CG A:LEU190 4.9 16.7 1.0

Chlorine binding site 2 out of 2 in the Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of A Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1525 b:28.1 occ:1.00 N B:ALA189 3.1 23.4 1.0 N B:TYR234 3.1 28.4 1.0 C B:GLU187 3.3 24.6 1.0 CA B:GLU187 3.3 22.8 1.0 CB B:ALA189 3.4 23.3 1.0 CD B:PRO188 3.4 25.4 1.0 N B:PRO188 3.4 25.0 1.0 CD2 B:TYR234 3.6 28.8 1.0 CA B:LEU233 3.6 26.1 1.0 CB B:ALA238 3.7 33.6 1.0 CA B:ALA189 3.7 24.7 1.0 CB B:GLU187 3.8 23.9 1.0 O B:GLU187 3.8 25.1 1.0 C B:LEU233 3.9 26.9 1.0 CB B:TYR234 3.9 29.1 1.0 CG B:PRO188 4.1 25.2 1.0 CD2 B:LEU233 4.1 26.6 1.0 CA B:TYR234 4.1 29.6 1.0 C B:PRO188 4.1 23.8 1.0 O B:VAL232 4.2 23.7 1.0 CG B:TYR234 4.2 28.1 1.0 N B:LEU190 4.3 27.4 1.0 CB B:LEU233 4.3 25.5 1.0 CA B:PRO188 4.3 24.0 1.0 C B:ALA189 4.4 26.2 1.0 N B:GLU187 4.6 22.3 1.0 CE2 B:TYR234 4.6 29.7 1.0 N B:LEU233 4.7 25.8 1.0 CG B:GLU187 4.7 22.5 1.0 C B:VAL232 4.8 26.2 1.0 CG B:LEU233 4.9 25.9 1.0 CG B:LEU190 4.9 26.2 1.0 CB B:PRO188 5.0 24.8 1.0

A.Ariza, J.M.Eklof, O.Spadiut, W.A.Offen, S.M.Roberts, W.Besenmatter, E.P.Friis, M.Skjot, K.S.Wilson, H.Brumer, G.Davies. Structure and Activity of Paenibacillus Polymyxa Xyloglucanase From Glycoside Hydrolase Family 44. J.Biol.Chem. V. 286 33890 2011.
ISSN: ISSN 0021-9258
PubMed: 21795708
DOI: 10.1074/JBC.M111.262345