Atomistry » Zinc » PDB 4uh1-4utr » 4uoq
Atomistry »
  Zinc »
    PDB 4uh1-4utr »
      4uoq »

Zinc in PDB 4uoq: Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04

Enzymatic activity of Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04

All present enzymatic activity of Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04:
3.2.1.23;

Protein crystallography data

The structure of Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04, PDB code: 4uoq was solved by A.H.Viborg, F.Fredslund, T.Katayama, S.K.Nielsen, B.Svensson, M.Kitaoka, L.Lo Leggio, M.Abou Hachem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.930 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 150.560, 150.560, 237.250, 90.00, 90.00, 120.00
R / Rfree (%) 18.09 / 22.67

Zinc Binding Sites:

The binding sites of Zinc atom in the Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 (pdb code 4uoq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04, PDB code: 4uoq:

Zinc binding site 1 out of 1 in 4uoq

Go back to Zinc Binding Sites List in 4uoq
Zinc binding site 1 out of 1 in the Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nucleophile Mutant (E324A) of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1702

b:77.7
occ:1.00
 NE2 A:HIS118 1.8 81.7 1.0
NE2 B:HIS118 1.8 82.3 1.0
NE2 C:HIS118 1.9 82.4 1.0
CE1 A:HIS118 2.3 80.3 1.0
O A:HOH2015 2.5 42.7 1.0
CE1 B:HIS118 2.7 80.1 1.0
CE1 C:HIS118 2.8 79.0 1.0
CD2 C:HIS118 2.9 76.8 1.0
CD2 B:HIS118 2.9 77.0 1.0
CD2 A:HIS118 3.1 73.5 1.0
ND1 A:HIS118 3.6 75.7 1.0
ND1 B:HIS118 3.8 75.4 1.0
CG A:HIS118 4.0 73.0 1.0
ND1 C:HIS118 4.0 73.7 1.0
CG B:HIS118 4.0 72.4 1.0
CG C:HIS118 4.0 75.5 1.0
OE1 A:GLN116 4.9 87.5 1.0
OE1 B:GLN116 4.9 96.5 1.0
CB C:GLN116 4.9 67.9 1.0

Reference:

A.H.Viborg, F.Fredslund, T.Katayama, S.K.Nielsen, B.Svensson, M.Kitaoka, L.L.Leggio, M.Abou Hachem. A BETA1-6/BETA1-3 Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 Gives Insight Into Sub-Specificities of Beta-Galactoside Catabolism Within Bifidobacterium. Mol.Microbiol. 2014.
ISSN: ESSN 1365-2958
PubMed: 25287704
DOI: 10.1111/MMI.12815
Page generated: Wed Aug 20 22:42:51 2025

Last articles

Zn in 5LOS
Zn in 5LMV
Zn in 5LMU
Zn in 5LMS
Zn in 5LMT
Zn in 5LMR
Zn in 5LMQ
Zn in 5LM6
Zn in 5LMP
Zn in 5LMO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy