Manganese in PDB 3oba: Structure of the Beta-Galactosidase From Kluyveromyces Lactis

All present enzymatic activity of Structure of the Beta-Galactosidase From Kluyveromyces Lactis:
3.2.1.23;

The structure of Structure of the Beta-Galactosidase From Kluyveromyces Lactis, PDB code: 3oba was solved by R.Fernandez-Leiro, A.Pereira-Rodriguez, M.Becerra, I.Gonzalez-Siso, M.E.Cerdan, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.57 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	140.030, 153.340, 216.160, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 24.3

The binding sites of Manganese atom in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis (pdb code 3oba). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis, PDB code: 3oba:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Beta-Galactosidase From Kluyveromyces Lactis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2001 b:8.2 occ:1.00 OD2 A:ASP978 1.8 13.4 1.0 OD2 A:ASP593 2.0 14.9 1.0 ND1 A:HIS975 2.0 10.3 1.0 CG A:ASP978 2.6 14.0 1.0 OD1 A:ASP978 2.8 15.0 1.0 CG A:ASP593 2.8 17.7 1.0 CE1 A:HIS975 2.9 9.4 1.0 OD1 A:ASP593 3.1 17.1 1.0 CG A:HIS975 3.1 11.4 1.0 CB A:HIS975 3.5 12.0 1.0 N A:HIS975 3.7 12.4 1.0 CB A:ALA974 3.8 12.9 1.0 CB A:ASP978 4.0 13.4 1.0 NE2 A:HIS975 4.1 9.3 1.0 O A:HOH1033 4.1 12.0 1.0 O A:VAL594 4.1 20.4 1.0 CD2 A:HIS975 4.2 10.1 1.0 CA A:HIS975 4.2 12.1 1.0 CB A:ASP593 4.2 18.4 1.0 C A:ALA974 4.3 12.8 1.0 SG A:CYS977 4.4 14.6 1.0 CA A:ALA974 4.4 13.0 1.0 N A:ALA974 4.6 13.6 1.0 O A:HIS975 5.0 12.2 1.0 C A:HIS975 5.0 12.2 1.0

Manganese binding site 2 out of 4 in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of the Beta-Galactosidase From Kluyveromyces Lactis within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn2001 b:8.9 occ:1.00 OD2 C:ASP593 1.9 15.0 1.0 OD2 C:ASP978 2.0 13.7 1.0 ND1 C:HIS975 2.1 10.3 1.0 CG C:ASP593 2.7 17.8 1.0 CG C:ASP978 2.7 14.0 1.0 OD1 C:ASP978 2.8 15.0 1.0 CE1 C:HIS975 2.9 9.4 1.0 OD1 C:ASP593 2.9 17.1 1.0 CG C:HIS975 3.2 11.4 1.0 CB C:HIS975 3.7 11.9 1.0 CB C:ALA974 3.9 12.8 1.0 N C:HIS975 3.9 12.4 1.0 O C:VAL594 4.0 20.4 1.0 NE2 C:HIS975 4.1 9.5 1.0 O C:HOH1179 4.1 25.9 1.0 CB C:ASP593 4.1 18.4 1.0 CB C:ASP978 4.2 13.3 1.0 CD2 C:HIS975 4.3 10.1 1.0 CA C:HIS975 4.4 12.1 1.0 C C:ALA974 4.5 12.8 1.0 SG C:CYS977 4.5 14.5 1.0 CA C:ALA974 4.6 13.1 1.0 N C:ALA974 4.8 13.7 1.0 C C:VAL594 4.9 20.6 1.0

Manganese binding site 3 out of 4 in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of the Beta-Galactosidase From Kluyveromyces Lactis within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn2001 b:11.3 occ:1.00 OD2 D:ASP593 1.8 14.9 1.0 OD2 D:ASP978 1.9 13.4 1.0 ND1 D:HIS975 2.0 10.4 1.0 CG D:ASP593 2.6 17.8 1.0 CG D:ASP978 2.7 14.0 1.0 OD1 D:ASP978 2.8 15.0 1.0 OD1 D:ASP593 2.9 17.3 1.0 CE1 D:HIS975 2.9 9.5 1.0 CG D:HIS975 3.1 11.4 1.0 CB D:HIS975 3.5 11.9 1.0 N D:HIS975 3.8 12.5 1.0 CB D:ALA974 4.0 13.0 1.0 O D:VAL594 4.0 20.5 1.0 CB D:ASP593 4.0 18.4 1.0 NE2 D:HIS975 4.1 9.4 1.0 CB D:ASP978 4.2 13.4 1.0 CD2 D:HIS975 4.2 10.1 1.0 CA D:HIS975 4.3 12.1 1.0 SG D:CYS977 4.3 14.4 1.0 C D:ALA974 4.4 12.8 1.0 CA D:ALA974 4.6 13.1 1.0 N D:ALA974 4.8 13.7 1.0 C D:VAL594 4.9 20.6 1.0

Manganese binding site 4 out of 4 in the Structure of the Beta-Galactosidase From Kluyveromyces Lactis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of the Beta-Galactosidase From Kluyveromyces Lactis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn2001 b:8.1 occ:1.00 OD2 B:ASP593 1.8 14.8 1.0 OD2 B:ASP978 1.9 13.4 1.0 ND1 B:HIS975 2.1 10.4 1.0 CG B:ASP978 2.6 14.0 1.0 CG B:ASP593 2.7 17.7 1.0 OD1 B:ASP978 2.8 14.9 1.0 OD1 B:ASP593 3.0 17.1 1.0 CE1 B:HIS975 3.0 9.5 1.0 CG B:HIS975 3.2 11.4 1.0 CB B:HIS975 3.6 11.9 1.0 N B:HIS975 3.8 12.4 1.0 CB B:ALA974 4.0 12.9 1.0 O B:VAL594 4.0 20.3 1.0 CB B:ASP978 4.1 13.4 1.0 CB B:ASP593 4.1 18.4 1.0 NE2 B:HIS975 4.2 9.5 1.0 CD2 B:HIS975 4.3 10.1 1.0 CA B:HIS975 4.3 12.1 1.0 SG B:CYS977 4.4 14.4 1.0 C B:ALA974 4.4 12.8 1.0 CA B:ALA974 4.6 13.0 1.0 N B:ALA974 4.7 13.6 1.0 C B:VAL594 4.9 20.6 1.0

A.Pereira-Rodriguez, R.Fernandez-Leiro, M.I.Gonzalez-Siso, M.E.Cerdan, M.Becerra, J.Sanz-Aparicio. Structural Basis of Specificity in Tetrameric Kluyveromyces Lactis Beta-Galactosidase. J.Struct.Biol. V. 177 392 2012.
ISSN: ISSN 1047-8477
PubMed: 22193516
DOI: 10.1016/J.JSB.2011.11.031