Atomistry » Chlorine » PDB 5ibn-5ilr » 5ift
Atomistry »
  Chlorine »
    PDB 5ibn-5ilr »
      5ift »

Chlorine in PDB 5ift: Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose

Enzymatic activity of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose

All present enzymatic activity of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose:
3.2.1.23;

Protein crystallography data

The structure of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose, PDB code: 5ift was solved by A.Rico-Diaz, M.Ramirez-Escudero, A.Vizoso Vazquez, M.E.Cerdan, M.Becerra, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.50 / 2.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 87.134, 111.641, 125.800, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 19.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose (pdb code 5ift). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose, PDB code: 5ift:

Chlorine binding site 1 out of 1 in 5ift

Go back to Chlorine Binding Sites List in 5ift
Chlorine binding site 1 out of 1 in the Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 3-B-Galactopyranosyl Glucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2003

b:20.3
occ:1.00
 O A:HOH4214 3.1 21.7 1.0
NE A:ARG862 3.2 17.1 1.0
N A:TYR1007 3.3 26.4 1.0
NE2 A:GLN863 3.3 18.0 1.0
NH2 A:ARG862 3.5 17.3 1.0
CZ A:ARG862 3.8 17.1 1.0
CB A:TYR1007 3.8 26.4 1.0
CD2 A:TYR1007 3.9 23.6 1.0
CB A:ALA1006 3.9 25.6 1.0
CA A:TYR1007 4.0 28.3 1.0
CB A:ARG862 4.0 16.8 1.0
CD1 A:TYR859 4.1 17.5 1.0
CG A:TYR1007 4.1 24.7 1.0
N A:HIS1008 4.2 38.3 1.0
CD A:ARG862 4.2 16.9 1.0
C A:ALA1006 4.2 25.7 1.0
CD A:GLN863 4.3 17.3 1.0
CA A:ALA1006 4.3 25.5 1.0
CG A:GLN863 4.5 17.2 1.0
C A:TYR1007 4.5 32.1 1.0
CE1 A:TYR859 4.6 17.6 1.0
O A:TYR859 4.7 15.7 1.0
CG A:ARG862 4.7 16.9 1.0
OH A:TYR690 4.7 23.3 1.0
CE2 A:TYR1007 4.8 23.1 1.0
CA A:TYR859 5.0 15.8 1.0

Reference:

A.Rico-Diaz, M.Ramirez-Escudero, A.Vizoso-Vazquez, M.E.Cerdan, M.Becerra, J.Sanz-Aparicio. Structural Features of Aspergillus Niger Beta-Galactosidase Define Its Activity Against Glycoside Linkages. Febs J. V. 284 1815 2017.
ISSN: ISSN 1742-4658
PubMed: 28391618
DOI: 10.1111/FEBS.14083
Page generated: Fri Jul 26 09:18:59 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy