Chlorine in PDB 2xvg: Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus

The structure of Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus, PDB code: 2xvg was solved by J.Larsbrink, A.Izumi, F.Ibatullin, A.Nakhai, H.J.Gilbert, G.J.Davies, H.Brumer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.885 / 2.60
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	156.193, 156.193, 227.759, 90.00, 90.00, 120.00
R / Rfree (%)	20.38 / 25.9

The structure of Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus also contains other interesting chemical elements:

Nickel

(Ni)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus (pdb code 2xvg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus, PDB code: 2xvg:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus


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 Alpha-Xylosidase (GH31) From Cellvibrio Japonicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1990 b:56.9 occ:1.00 NI A:NI1998 2.3 44.7 1.0 CL A:CL1993 2.6 69.5 1.0 CL A:CL1991 2.8 64.9 1.0 CL A:CL1992 3.8 56.5 1.0 OE1 A:GLU885 3.8 43.2 1.0 NE2 A:HIS882 3.8 48.2 1.0 CD A:GLU885 3.8 49.4 1.0 OE2 A:GLU885 4.1 51.5 1.0 CG A:GLU885 4.2 47.5 1.0 CB A:GLU885 4.4 42.8 1.0 CE1 A:HIS882 4.6 49.4 1.0 CD2 A:HIS882 4.7 37.3 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus


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 Alpha-Xylosidase (GH31) From Cellvibrio Japonicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1991 b:64.9 occ:1.00 NI A:NI1998 2.2 44.7 1.0 CL A:CL1990 2.8 56.9 1.0 OD1 A:ASN503 3.1 64.2 1.0 CL A:CL1992 3.2 56.5 1.0 CG A:ASN503 3.3 60.1 1.0 NE2 A:HIS882 3.4 48.2 1.0 ND2 A:ASN503 3.5 58.1 1.0 CE1 A:HIS882 3.9 49.4 1.0 CL A:CL1993 4.1 69.5 1.0 CB A:ASN503 4.2 50.2 1.0 CD2 A:HIS882 4.6 37.3 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus


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 Alpha-Xylosidase (GH31) From Cellvibrio Japonicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1992 b:56.5 occ:1.00 NI A:NI1998 2.3 44.7 1.0 CL A:CL1993 2.6 69.5 1.0 OD1 A:ASN503 3.2 64.2 1.0 CL A:CL1991 3.2 64.9 1.0 CL A:CL1990 3.8 56.9 1.0 NE2 A:HIS882 3.9 48.2 1.0 CG A:ASN503 4.1 60.1 1.0 CD2 A:HIS882 4.2 37.3 1.0 NE A:ARG458 4.4 38.2 1.0 CD A:ARG458 4.6 36.5 1.0 CB A:ASN503 4.7 50.2 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Alpha-Xylosidase (GH31) From Cellvibrio Japonicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1993 b:69.5 occ:1.00 NI A:NI1998 2.3 44.7 1.0 CL A:CL1990 2.6 56.9 1.0 CL A:CL1992 2.6 56.5 1.0 OE1 A:GLU885 3.1 43.2 1.0 CD A:GLU885 3.7 49.4 1.0 NE2 A:HIS882 3.8 48.2 1.0 CG A:GLN881 3.8 61.7 1.0 CB A:GLN881 3.9 57.1 1.0 OE2 A:GLU885 4.0 51.5 1.0 CD2 A:HIS882 4.0 37.3 1.0 CL A:CL1991 4.1 64.9 1.0 CG A:GLU885 4.9 47.5 1.0 CD A:GLN881 5.0 68.2 1.0 N A:GLN881 5.0 47.6 1.0

J.Larsbrink, A.Izumi, F.Ibatullin, A.Nakhai, H.J.Gilbert, G.J.Davies, H.Brumer. Structural and Enzymatic Characterisation of A Glycoside Hydrolase Family 31 Alpha-Xylosidase From Cellvibrio Japonicus Involved in Xyloglucan Saccharification. Biochem.J. V. 436 567 2011.
ISSN: ISSN 0264-6021
PubMed: 21426303
DOI: 10.1042/BJ20110299