Manganese in PDB 8bvk: The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge

The structure of The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge, PDB code: 8bvk was solved by K.Kuhlmann, J.Bitter, M.Pfeiffer, B.Nidetzky, T.Pavkov-Keller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.84 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.58, 93.67, 123.68, 90, 90, 90
R / Rfree (%)	17.4 / 21.8

The binding sites of Manganese atom in the The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge (pdb code 8bvk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge, PDB code: 8bvk:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:35.9 occ:0.53 NE2 A:HIS66 2.0 34.0 1.0 ND1 A:HIS132 2.3 34.7 1.0 OE2 A:GLU161 2.4 36.7 1.0 CE1 A:HIS66 2.7 34.6 1.0 CD2 A:HIS66 3.1 31.6 1.0 OE1 A:GLU39 3.1 30.7 1.0 CG A:HIS132 3.1 26.0 1.0 CE1 A:HIS132 3.2 36.4 1.0 CB A:HIS132 3.4 22.2 1.0 CD A:GLU161 3.5 34.1 1.0 OE2 A:GLU39 3.6 35.1 1.0 CD A:GLU39 3.7 29.0 1.0 ND1 A:HIS66 3.9 34.3 1.0 CG A:HIS66 4.1 32.3 1.0 CD2 A:HIS132 4.2 28.1 1.0 NE2 A:HIS132 4.2 31.5 1.0 ND1 A:HIS189 4.2 37.8 1.0 CG2 A:THR92 4.2 23.3 1.0 OE1 A:GLU161 4.3 38.0 1.0 CE1 A:HIS189 4.3 34.9 1.0 OE1 A:GLN13 4.5 39.3 1.0 CG A:GLU161 4.5 29.3 1.0 CA A:PRO94 4.6 25.3 1.0 CB A:PRO94 4.8 26.0 1.0 O A:PRO94 4.8 34.0 1.0 CA A:HIS132 4.9 22.0 1.0 CG A:GLU39 4.9 28.2 1.0

Manganese binding site 2 out of 3 in the The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:19.0 occ:0.98 OE1 A:GLU148 1.9 25.3 1.0 OD2 A:ASP152 2.0 23.2 1.0 CD A:GLU148 2.9 28.1 1.0 CG A:ASP152 3.0 21.0 1.0 OD1 A:ASP152 3.3 20.2 1.0 CG A:GLU148 3.4 22.0 1.0 OE2 A:GLU148 4.0 25.9 1.0 O A:HOH468 4.0 20.2 1.0 CB A:ASP152 4.3 18.4 1.0 NH2 A:ARG184 4.5 22.2 1.0 NZ A:LYS144 4.7 27.1 1.0 CE A:LYS144 4.8 27.1 1.0 CB A:GLU148 4.9 20.3 1.0 O A:GLU148 5.0 21.2 1.0

Manganese binding site 3 out of 3 in the The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of The Crystal Structure of O-Glycoside Cleaving Beta-Eliminase From A. Tumefaciens Atoge within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn301 b:62.3 occ:0.50 NE2 B:HIS132 2.0 34.6 1.0 ND1 B:HIS189 2.3 38.0 1.0 OD2 B:ASP163 2.4 35.8 1.0 O B:HOH402 2.5 40.6 1.0 CE1 B:HIS132 2.5 32.1 1.0 CE1 B:HIS189 2.7 37.8 1.0 O B:HOH452 2.9 44.0 1.0 CG B:HIS189 3.0 29.8 1.0 CD2 B:HIS132 3.1 29.1 1.0 OE1 B:GLU233 3.1 41.7 1.0 NE2 B:HIS189 3.5 37.1 1.0 CG B:ASP163 3.5 31.1 1.0 CD2 B:HIS189 3.7 36.5 1.0 CB B:HIS189 3.7 26.6 1.0 ND1 B:HIS132 3.7 34.2 1.0 CG B:HIS132 4.0 26.0 1.0 CB B:ASP163 4.1 23.7 1.0 O B:HOH493 4.2 42.9 1.0 CD B:GLU233 4.4 49.2 1.0 OD1 B:ASP163 4.5 30.5 1.0 O B:ASN133 4.8 22.7 1.0 CA B:HIS189 4.9 23.8 1.0

J.Bitter, M.Pfeiffer, A.J.E.Borg, K.Kuhlmann, T.Pavkov-Keller, B.Nidetzky. Enzymatic Beta-Elimination in Natural Product Deglycosylation: C-C Bond Cleavage As A Specialty of A Conserved Mechanism To Be Published.