Manganese in PDB 8suu: Crystal Structure of Yisk From Bacillus Subtilis in Apo Form

The structure of Crystal Structure of Yisk From Bacillus Subtilis in Apo Form, PDB code: 8suu was solved by I.V.Krieger, V.Chemelewski, T.Guo, A.Sperber, J.Herman, J.C.Sacchettini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.93 / 2.26
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.937, 93.768, 125.484, 90, 90, 90
R / Rfree (%)	21.1 / 25.5

The binding sites of Manganese atom in the Crystal Structure of Yisk From Bacillus Subtilis in Apo Form (pdb code 8suu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Yisk From Bacillus Subtilis in Apo Form, PDB code: 8suu:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Yisk From Bacillus Subtilis in Apo Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Yisk From Bacillus Subtilis in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:89.9 occ:1.00 O A:HOH527 2.1 64.0 1.0 OE1 A:GLU148 2.2 62.5 1.0 OE2 A:GLU150 2.2 60.2 1.0 OD2 A:ASP179 2.2 48.8 1.0 O A:HOH509 2.7 50.3 1.0 CD A:GLU150 3.3 54.5 1.0 CG A:ASP179 3.3 49.0 1.0 CD A:GLU148 3.4 54.6 1.0 O A:HOH530 3.5 54.5 1.0 OE1 A:GLU150 3.7 55.0 1.0 CB A:ASP179 3.8 48.7 1.0 O A:ILE97 3.8 63.1 1.0 NZ A:LYS196 3.9 51.9 1.0 OE2 A:GLU148 4.0 54.3 1.0 CZ A:PHE121 4.2 50.5 1.0 OD1 A:ASP179 4.4 47.5 1.0 CB A:GLU148 4.4 50.8 1.0 CE A:LYS196 4.4 50.3 1.0 CG A:GLU148 4.5 54.6 1.0 CG A:GLU150 4.6 51.4 1.0 N A:THR266 4.7 49.8 1.0 CE1 A:PHE121 4.8 47.6 1.0 CA A:GLY265 4.8 50.1 1.0 CG2 A:THR266 4.8 53.2 1.0 CB A:THR266 4.8 51.8 1.0 O A:ASP179 5.0 50.0 1.0 C A:ILE97 5.0 60.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Yisk From Bacillus Subtilis in Apo Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Yisk From Bacillus Subtilis in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:113.8 occ:1.00 O B:HOH505 2.1 55.4 1.0 OD2 B:ASP179 2.2 65.6 1.0 OE1 B:GLU148 2.3 69.3 1.0 OE2 B:GLU150 2.3 58.9 1.0 O B:HOH519 2.8 53.2 1.0 O B:HOH517 2.9 62.7 1.0 CG B:ASP179 3.3 62.0 1.0 CD B:GLU150 3.4 58.2 1.0 CD B:GLU148 3.5 68.1 1.0 O B:ILE97 3.7 62.5 1.0 OE1 B:GLU150 3.7 57.5 1.0 CB B:ASP179 3.9 58.8 1.0 NZ B:LYS196 3.9 72.7 1.0 CZ B:PHE121 4.0 61.9 1.0 OE2 B:GLU148 4.1 72.6 1.0 OD1 B:ASP179 4.4 65.2 1.0 CE B:LYS196 4.4 68.1 1.0 CB B:GLU148 4.6 63.0 1.0 CG B:GLU148 4.6 66.7 1.0 CE1 B:PHE121 4.6 61.3 1.0 CG B:GLU150 4.7 58.7 1.0 N B:THR266 4.7 61.8 1.0 CA B:GLY265 4.8 59.4 1.0 C B:ILE97 4.9 62.0 1.0 CG2 B:THR266 4.9 62.5 1.0 CB B:THR266 5.0 62.2 1.0 CB B:CYS96 5.0 54.7 1.0

T.Guo, J.Herman. Bacillus Subtilis Yisk Possesses Oxaloacetate Decarboxylase Activity and Exhibits Mbl-Dependent Localization To Be Published.