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Chlorine in PDB 5mgd: Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose

Enzymatic activity of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose

All present enzymatic activity of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose:
3.2.1.23;

Protein crystallography data

The structure of Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose, PDB code: 5mgd 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) 82.63 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.285, 105.873, 83.715, 90.00, 99.24, 90.00
R / Rfree (%) 19.1 / 22.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose (pdb code 5mgd). 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 6-Galactosyl-Lactose, PDB code: 5mgd:

Chlorine binding site 1 out of 1 in 5mgd

Go back to Chlorine Binding Sites List in 5mgd
Chlorine binding site 1 out of 1 in the Structure of E298Q-Beta-Galactosidase From Aspergillus Niger in Complex with 6-Galactosyl-Lactose


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 6-Galactosyl-Lactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl3002

b:26.6
occ:1.00
 NE A:ARG862 3.2 22.7 1.0
N A:TYR1007 3.3 32.7 1.0
NH2 A:ARG862 3.3 22.9 1.0
NE2 A:GLN863 3.3 24.0 1.0
CB A:TYR1007 3.6 31.0 1.0
CZ A:ARG862 3.7 23.2 1.0
CA A:TYR1007 3.8 33.9 1.0
N A:HIS1008 3.9 42.6 1.0
CD2 A:TYR1007 3.9 28.6 1.0
CB A:ARG862 3.9 21.6 1.0
CD1 A:TYR859 4.0 22.5 1.0
CG A:TYR1007 4.1 29.2 1.0
CB A:ALA1006 4.1 33.7 1.0
C A:TYR1007 4.2 37.5 1.0
CD A:GLN863 4.3 23.9 1.0
CD A:ARG862 4.3 22.4 1.0
CE1 A:TYR859 4.3 23.0 1.0
C A:ALA1006 4.3 33.4 1.0
CG A:GLN863 4.4 22.9 1.0
CA A:ALA1006 4.5 34.9 1.0
CG A:ARG862 4.7 21.9 1.0
O A:TYR859 4.7 18.6 1.0
CA A:HIS1008 4.8 49.4 1.0
OH A:TYR690 4.9 26.7 1.0
CB A:HIS1008 4.9 55.5 1.0
CE2 A:TYR1007 5.0 27.2 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: Sat Jul 12 05:28:38 2025

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