Manganese in PDB 2qun: Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose

The structure of Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose, PDB code: 2qun was solved by H.Yoshida, M.Yamada, T.Nishitani, G.Takada, K.Izumori, S.Kamitori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.30 / 2.06
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.203, 139.927, 92.194, 90.00, 104.86, 90.00
R / Rfree (%)	16.9 / 21.3

The binding sites of Manganese atom in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose (pdb code 2qun). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose, PDB code: 2qun:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose


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 D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn292 b:16.9 occ:1.00 OE2 A:GLU152 2.1 15.8 1.0 OD2 A:ASP185 2.2 11.6 1.0 O2 A:FUD291 2.2 31.0 1.0 ND1 A:HIS211 2.2 13.4 1.0 OE1 A:GLU246 2.4 22.0 1.0 O3 A:FUD291 2.9 39.1 1.0 C2 A:FUD291 3.0 35.8 1.0 CD A:GLU152 3.2 17.1 1.0 CE1 A:HIS211 3.2 15.0 1.0 C3 A:FUD291 3.2 40.0 1.0 CG A:HIS211 3.3 15.4 1.0 CG A:ASP185 3.3 15.2 1.0 CD A:GLU246 3.4 23.0 1.0 OE1 A:GLU152 3.5 14.7 1.0 CB A:HIS211 3.6 13.6 1.0 OE2 A:GLU246 3.6 26.8 1.0 CB A:ASP185 3.8 12.5 1.0 O A:HOH327 4.1 21.8 1.0 NH2 A:ARG217 4.2 17.4 1.0 CD2 A:HIS188 4.3 9.0 1.0 NE2 A:HIS211 4.3 14.7 1.0 OD1 A:ASP185 4.3 16.0 1.0 NE2 A:HIS188 4.3 9.3 1.0 NE2 A:GLN183 4.4 17.4 1.0 CD2 A:HIS211 4.4 15.6 1.0 C1 A:FUD291 4.4 31.5 1.0 CG A:GLU152 4.5 14.6 1.0 C4 A:FUD291 4.7 44.0 1.0 CG A:GLU246 4.7 23.5 1.0 O1 A:FUD291 5.0 25.4 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose


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 D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn292 b:16.0 occ:1.00 OE2 B:GLU152 2.1 16.1 1.0 OD2 B:ASP185 2.1 9.8 1.0 ND1 B:HIS211 2.2 9.8 1.0 O2 B:FUD291 2.2 31.1 1.0 OE1 B:GLU246 2.5 15.6 1.0 O3 B:FUD291 2.8 43.1 1.0 C2 B:FUD291 3.0 37.5 1.0 C3 B:FUD291 3.0 43.1 1.0 CE1 B:HIS211 3.1 15.6 1.0 CD B:GLU152 3.2 17.2 1.0 CG B:HIS211 3.3 14.6 1.0 CG B:ASP185 3.3 10.1 1.0 CD B:GLU246 3.3 18.8 1.0 OE2 B:GLU246 3.5 23.2 1.0 OE1 B:GLU152 3.6 17.9 1.0 CB B:HIS211 3.6 11.9 1.0 CB B:ASP185 3.9 11.7 1.0 NH2 B:ARG217 4.1 17.5 1.0 O B:HOH451 4.2 17.9 1.0 NE2 B:HIS211 4.3 15.5 1.0 NE2 B:GLN183 4.3 14.3 1.0 OD1 B:ASP185 4.3 11.3 1.0 CD2 B:HIS188 4.3 12.1 1.0 NE2 B:HIS188 4.3 9.3 1.0 CD2 B:HIS211 4.4 12.7 1.0 C1 B:FUD291 4.4 34.4 1.0 CG B:GLU152 4.5 13.3 1.0 C4 B:FUD291 4.6 48.2 1.0 CG B:GLU246 4.7 19.8 1.0 O1 B:FUD291 4.9 25.8 1.0 O5 B:FUD291 5.0 53.2 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn292 b:15.6 occ:1.00 OD2 C:ASP185 2.1 10.2 1.0 OE2 C:GLU152 2.2 14.4 1.0 O2 C:FUD291 2.3 24.6 1.0 ND1 C:HIS211 2.3 11.8 1.0 OE1 C:GLU246 2.4 16.4 1.0 O3 C:FUD291 2.8 36.0 1.0 C2 C:FUD291 3.1 31.8 1.0 CE1 C:HIS211 3.2 13.5 1.0 C3 C:FUD291 3.2 37.9 1.0 CD C:GLU152 3.2 14.0 1.0 CG C:ASP185 3.3 12.7 1.0 CD C:GLU246 3.3 16.1 1.0 CG C:HIS211 3.3 13.4 1.0 OE2 C:GLU246 3.5 23.7 1.0 OE1 C:GLU152 3.6 13.2 1.0 CB C:HIS211 3.6 10.2 1.0 CB C:ASP185 3.9 13.2 1.0 NH2 C:ARG217 4.0 13.2 1.0 O C:HOH313 4.2 14.5 1.0 NE2 C:GLN183 4.3 12.2 1.0 OD1 C:ASP185 4.3 13.2 1.0 NE2 C:HIS211 4.3 14.8 1.0 CD2 C:HIS188 4.4 11.8 1.0 NE2 C:HIS188 4.4 11.7 1.0 CD2 C:HIS211 4.4 13.2 1.0 C1 C:FUD291 4.5 29.2 1.0 CG C:GLU152 4.6 10.5 1.0 CG C:GLU246 4.7 19.0 1.0 C4 C:FUD291 4.7 44.4 1.0 O5 C:FUD291 4.8 50.7 1.0 O1 C:FUD291 4.9 24.0 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of D-Tagatose 3-Epimerase From Pseudomonas Cichorii in Complex with D-Fructose within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn292 b:15.1 occ:1.00 OD2 D:ASP185 2.1 9.8 1.0 OE2 D:GLU152 2.2 14.8 1.0 ND1 D:HIS211 2.2 8.8 1.0 O2 D:FUD291 2.3 27.6 1.0 OE1 D:GLU246 2.4 20.1 1.0 O3 D:FUD291 2.8 34.6 1.0 CE1 D:HIS211 3.1 14.7 1.0 C2 D:FUD291 3.2 32.0 1.0 CD D:GLU152 3.2 15.1 1.0 CG D:ASP185 3.3 11.5 1.0 CG D:HIS211 3.3 13.2 1.0 CD D:GLU246 3.3 20.3 1.0 C3 D:FUD291 3.4 36.4 1.0 OE2 D:GLU246 3.5 23.4 1.0 OE1 D:GLU152 3.6 14.0 1.0 CB D:HIS211 3.6 10.0 1.0 CB D:ASP185 3.9 10.7 1.0 NH2 D:ARG217 4.2 18.6 1.0 O D:HOH339 4.2 18.4 1.0 OD1 D:ASP185 4.3 11.4 1.0 NE2 D:HIS211 4.3 13.1 1.0 CD2 D:HIS188 4.3 8.4 1.0 NE2 D:GLN183 4.3 15.3 1.0 NE2 D:HIS188 4.4 11.2 1.0 CD2 D:HIS211 4.4 12.2 1.0 CG D:GLU152 4.5 12.6 1.0 C1 D:FUD291 4.6 28.6 1.0 CG D:GLU246 4.7 21.0 1.0 O1 D:FUD291 4.8 23.7 1.0 C4 D:FUD291 4.9 40.6 1.0 O5 D:FUD291 5.0 46.8 1.0

H.Yoshida, M.Yamada, T.Nishitani, G.Takada, K.Izumori, S.Kamitori. Crystal Structures of D-Tagatose 3-Epimerase From Pseudomonas Cichorii and Its Complexes with D-Tagatose and D-Fructose J.Mol.Biol. V. 374 443 2007.
ISSN: ISSN 0022-2836
PubMed: 17936787
DOI: 10.1016/J.JMB.2007.09.033