Manganese in PDB 3pzt: Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion

All present enzymatic activity of Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion:
3.2.1.4;

The structure of Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion, PDB code: 3pzt was solved by C.R.Santos, J.H.Paiva, P.K.Akao, A.N.Meza, J.C.Silva, F.M.Squina, R.J.Ward, R.Ruller, M.T.Murakami, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.40 / 1.97
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.526, 110.617, 122.262, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 20.6

The binding sites of Manganese atom in the Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion (pdb code 3pzt). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion, PDB code: 3pzt:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion


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 Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1 b:48.5 occ:1.00 OD2 A:ASP197 2.2 42.7 1.0 O A:HOH532 2.4 38.0 1.0 OD1 A:ASP195 2.4 26.6 1.0 O A:HOH339 2.5 53.7 1.0 OD1 A:ASN198 3.2 34.9 1.0 O A:GLY157 3.2 36.8 1.0 CG A:ASN198 3.2 26.7 1.0 CG A:ASP195 3.3 28.6 1.0 CG A:ASP197 3.3 37.7 1.0 ND2 A:ASN198 3.4 36.7 1.0 OD2 A:ASP195 3.7 26.3 1.0 N A:ASN198 3.7 24.8 1.0 OD1 A:ASP197 3.8 46.0 1.0 C A:GLY157 4.1 35.0 1.0 N A:ASP197 4.1 29.1 1.0 CB A:ASN198 4.1 23.7 1.0 OE1 A:GLN41 4.2 32.2 1.0 C A:ASP197 4.4 28.7 1.0 CA A:ASN198 4.4 24.8 1.0 CD A:PRO196 4.5 28.8 1.0 CA A:ASP197 4.5 29.3 1.0 CB A:ASP197 4.5 33.0 1.0 CB A:ASP195 4.5 28.7 1.0 NE2 A:GLN41 4.5 24.6 1.0 CA A:ASP195 4.5 27.6 1.0 N A:PRO196 4.6 28.2 1.0 C A:ASP195 4.7 28.1 1.0 CD A:GLN41 4.7 31.8 1.0 CA A:ASN158 4.8 34.4 1.0 N A:ASN158 4.8 33.8 1.0 CA A:GLY157 4.8 33.3 1.0 O A:THR159 5.0 32.8 1.0 N A:THR159 5.0 31.9 1.0

Manganese binding site 2 out of 2 in the Structure of the Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion


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 Endo-1,4-Beta-Glucanase From Bacillus Subtilis 168 with Manganese(II) Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn2 b:52.0 occ:1.00 O B:HOH489 2.0 34.8 1.0 OD1 B:ASP195 2.4 35.0 1.0 OD2 B:ASP197 2.4 40.2 1.0 O B:GLY157 2.5 44.8 1.0 O B:HOH557 2.6 45.0 1.0 CG B:ASP195 3.2 32.8 1.0 CG B:ASP197 3.5 40.0 1.0 CG B:ASN198 3.5 34.2 1.0 OD2 B:ASP195 3.6 34.0 1.0 ND2 B:ASN198 3.6 37.8 1.0 OD1 B:ASN198 3.6 41.1 1.0 C B:GLY157 3.7 42.5 1.0 OD1 B:ASP197 4.0 44.6 1.0 N B:ASN198 4.0 29.6 1.0 OE1 B:GLN41 4.2 34.6 1.0 CB B:ASN198 4.2 27.8 1.0 N B:ASP197 4.3 33.0 1.0 CB B:ASP195 4.4 34.5 1.0 CA B:ASP195 4.4 35.1 1.0 CA B:ASN158 4.4 42.2 1.0 CD B:PRO196 4.5 38.0 1.0 N B:ASN158 4.5 42.1 1.0 N B:PRO196 4.6 36.1 1.0 CA B:ASN198 4.6 28.0 1.0 C B:ASP195 4.6 35.7 1.0 CA B:GLY157 4.6 41.0 1.0 C B:ASP197 4.6 30.6 1.0 NE2 B:GLN41 4.7 29.6 1.0 CA B:ASP197 4.7 32.0 1.0 CB B:ASP197 4.7 33.4 1.0 C B:ASN158 4.7 41.2 1.0 N B:THR159 4.8 37.9 1.0 O B:THR159 4.8 38.2 1.0 CD B:GLN41 4.8 34.1 1.0

C.R.Santos, J.H.Paiva, M.L.Sforca, J.L.Neves, R.Z.Navarro, J.Cota, P.K.Akao, Z.B.Hoffmam, A.N.Meza, J.H.Smetana, M.L.Nogueira, I.Polikarpov, J.Xavier-Neto, F.M.Squina, R.J.Ward, R.Ruller, A.C.Zeri, M.T.Murakami. Dissecting Structure-Function-Stability Relationships of A Thermostable GH5-CBM3 Cellulase From Bacillus Subtilis 168. Biochem.J. V. 441 95 2012.
ISSN: ISSN 0264-6021
PubMed: 21880019
DOI: 10.1042/BJ20110869