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

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

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

Protein crystallography data

The structure of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 Nucleophile Mutant E324A in Complex with Galactose, PDB code: 4uoz 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) 28.68 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 134.200, 167.970, 108.580, 90.00, 115.64, 90.00
R / Rfree (%) 18.613 / 24.813

Zinc Binding Sites:

The binding sites of Zinc atom in the Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 Nucleophile Mutant E324A in Complex with Galactose (pdb code 4uoz). 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 Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 Nucleophile Mutant E324A in Complex with Galactose, PDB code: 4uoz:

Zinc binding site 1 out of 1 in 4uoz

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Beta-(1,6)-Galactosidase From Bifidobacterium Animalis Subsp. Lactis Bl-04 Nucleophile Mutant E324A in Complex with Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1696

b:43.2
occ:1.00
 NE2 A:HIS118 2.0 35.5 1.0
NE2 C:HIS118 2.1 29.8 1.0
NE2 B:HIS118 2.3 41.2 1.0
CE1 A:HIS118 3.0 35.8 1.0
CD2 B:HIS118 3.0 37.9 1.0
CD2 C:HIS118 3.0 30.4 1.0
CD2 A:HIS118 3.0 33.6 1.0
CE1 C:HIS118 3.1 30.1 1.0
CE1 B:HIS118 3.5 39.1 1.0
O B:HOH2052 3.9 33.1 1.0
OE1 A:GLN116 4.1 38.0 1.0
ND1 A:HIS118 4.1 34.4 1.0
OE1 B:GLN116 4.2 45.2 1.0
CG A:HIS118 4.2 35.1 1.0
CG C:HIS118 4.2 29.9 1.0
ND1 C:HIS118 4.2 29.9 1.0
OE1 C:GLN116 4.3 33.7 1.0
CG B:HIS118 4.3 37.2 1.0
ND1 B:HIS118 4.5 38.6 1.0
CD A:GLN116 4.6 41.2 1.0
CB A:GLN116 4.7 38.5 1.0
CD C:GLN116 4.7 35.1 1.0
CD B:GLN116 4.8 41.2 1.0
CB B:GLN116 4.8 37.2 1.0
CB C:GLN116 4.8 31.3 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: Sun Oct 27 09:12:58 2024

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