Manganese in PDB 4xsm: Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol

The structure of Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol, PDB code: 4xsm was solved by H.Yoshida, A.Yoshihara, T.Ishii, K.Izumori, S.Kamitori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.68 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.430, 127.030, 98.830, 90.00, 101.33, 90.00
R / Rfree (%)	24.5 / 30.7

The binding sites of Manganese atom in the Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol (pdb code 4xsm). 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 C66S From Pseudomonas Cichorii in Complex with D-Talitol, PDB code: 4xsm:
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 C66S From Pseudomonas Cichorii in Complex with D-Talitol


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 C66S From Pseudomonas Cichorii in Complex with D-Talitol within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:32.8 occ:1.00 OD2 A:ASP185 2.1 28.0 1.0 OE2 A:GLU152 2.1 29.8 1.0 ND1 A:HIS211 2.2 29.9 1.0 O5 A:TLZ402 2.3 45.3 1.0 O4 A:TLZ402 2.5 54.5 1.0 OE1 A:GLU246 3.0 37.4 1.0 C5 A:TLZ402 3.0 49.5 1.0 CD A:GLU152 3.1 30.5 1.0 CG A:HIS211 3.1 33.0 1.0 CE1 A:HIS211 3.2 31.6 1.0 C4 A:TLZ402 3.2 52.3 1.0 CG A:ASP185 3.3 26.9 1.0 CB A:HIS211 3.4 31.4 1.0 OE1 A:GLU152 3.4 31.4 1.0 CD A:GLU246 3.8 35.5 1.0 C3 A:TLZ402 3.9 55.3 1.0 CB A:ASP185 3.9 28.5 1.0 OE2 A:GLU246 4.0 37.5 1.0 CD2 A:HIS188 4.2 21.1 1.0 NE2 A:HIS211 4.3 33.9 1.0 CD2 A:HIS211 4.3 34.2 1.0 OD1 A:ASP185 4.3 28.8 1.0 NE2 A:HIS188 4.3 23.0 1.0 NE2 A:GLN183 4.3 19.8 1.0 CG A:GLU152 4.4 30.3 1.0 C6 A:TLZ402 4.4 49.3 1.0 O3 A:TLZ402 4.5 58.6 1.0 O6 A:TLZ402 4.7 53.0 1.0 NH2 A:ARG217 4.8 28.3 1.0 O A:HOH520 4.9 18.2 1.0 CA A:HIS211 4.9 30.9 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol


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 C66S From Pseudomonas Cichorii in Complex with D-Talitol within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:33.7 occ:1.00 O5 B:TLZ402 2.1 60.7 1.0 OE2 B:GLU152 2.1 26.9 1.0 OD2 B:ASP185 2.1 27.1 1.0 ND1 B:HIS211 2.4 32.0 1.0 C5 B:TLZ402 2.7 58.7 1.0 OE1 B:GLU246 2.9 36.1 1.0 CD B:GLU152 3.1 28.7 1.0 CG B:ASP185 3.2 25.9 1.0 O4 B:TLZ402 3.2 59.2 1.0 CE1 B:HIS211 3.2 33.3 1.0 OE1 B:GLU152 3.4 29.6 1.0 C4 B:TLZ402 3.5 59.7 1.0 CG B:HIS211 3.5 32.8 1.0 CB B:ASP185 3.7 27.2 1.0 CD B:GLU246 3.8 32.2 1.0 CB B:HIS211 3.8 32.9 1.0 NE2 B:HIS188 3.9 22.7 1.0 OE2 B:GLU246 4.0 33.4 1.0 O B:HOH569 4.0 26.9 1.0 C6 B:TLZ402 4.1 58.0 1.0 CD2 B:HIS188 4.1 23.5 1.0 C3 B:TLZ402 4.1 59.7 1.0 OD1 B:ASP185 4.3 28.0 1.0 O6 B:TLZ402 4.3 53.3 1.0 NE2 B:GLN183 4.3 32.4 1.0 O3 B:TLZ402 4.4 61.1 1.0 CG B:GLU152 4.4 26.2 1.0 NE2 B:HIS211 4.4 35.0 1.0 NH2 B:ARG217 4.4 31.2 1.0 CD2 B:HIS211 4.5 34.2 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol


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 C66S From Pseudomonas Cichorii in Complex with D-Talitol within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:35.3 occ:1.00 O5 C:TLZ402 2.1 52.9 1.0 OE2 C:GLU152 2.3 31.7 1.0 OD2 C:ASP185 2.3 28.0 1.0 ND1 C:HIS211 2.4 33.1 1.0 C5 C:TLZ402 2.8 53.6 1.0 OE1 C:GLU246 2.9 42.2 1.0 CD C:GLU152 3.0 28.3 1.0 O4 C:TLZ402 3.1 58.0 1.0 CE1 C:HIS211 3.2 33.2 1.0 CG C:ASP185 3.3 28.8 1.0 OE1 C:GLU152 3.3 30.5 1.0 C4 C:TLZ402 3.4 55.6 1.0 CG C:HIS211 3.4 32.3 1.0 CB C:ASP185 3.6 30.2 1.0 CB C:HIS211 3.7 31.1 1.0 CD C:GLU246 4.0 40.8 1.0 C3 C:TLZ402 4.0 56.7 1.0 CD2 C:HIS188 4.0 30.0 1.0 NE2 C:HIS188 4.1 28.5 1.0 NE2 C:GLN183 4.1 40.6 1.0 C6 C:TLZ402 4.2 51.8 1.0 OE2 C:GLU246 4.3 43.2 1.0 CG C:GLU152 4.3 28.1 1.0 NH2 C:ARG217 4.4 27.4 1.0 O3 C:TLZ402 4.4 57.0 1.0 O6 C:TLZ402 4.4 50.9 1.0 OD1 C:ASP185 4.4 28.6 1.0 NE2 C:HIS211 4.4 33.0 1.0 CD2 C:HIS211 4.5 33.2 1.0 CA C:ASP185 5.0 30.8 1.0 O C:HOH521 5.0 34.3 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of D-Tagatose 3-Epimerase C66S From Pseudomonas Cichorii in Complex with D-Talitol


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 C66S From Pseudomonas Cichorii in Complex with D-Talitol within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn401 b:47.0 occ:1.00 OD2 D:ASP185 2.1 39.1 1.0 OE2 D:GLU152 2.2 42.6 1.0 O5 D:TLZ402 2.3 62.2 1.0 O4 D:TLZ402 2.4 65.5 1.0 ND1 D:HIS211 2.4 42.3 1.0 OE1 D:GLU246 3.1 38.0 1.0 CD D:GLU152 3.1 43.4 1.0 CG D:ASP185 3.1 38.6 1.0 C5 D:TLZ402 3.2 61.9 1.0 C4 D:TLZ402 3.2 63.9 1.0 CE1 D:HIS211 3.4 41.7 1.0 CG D:HIS211 3.4 41.7 1.0 OE1 D:GLU152 3.4 43.4 1.0 CB D:ASP185 3.6 38.7 1.0 CB D:HIS211 3.6 41.3 1.0 CD D:GLU246 3.9 38.3 1.0 O D:HOH548 3.9 25.8 1.0 OE2 D:GLU246 4.0 41.9 1.0 C3 D:TLZ402 4.0 64.0 1.0 OD1 D:ASP185 4.2 40.4 1.0 O3 D:TLZ402 4.2 65.3 1.0 NH2 D:ARG217 4.3 31.8 1.0 NE2 D:GLN183 4.3 36.1 1.0 CG D:GLU152 4.4 42.0 1.0 CD2 D:HIS188 4.4 35.5 1.0 NE2 D:HIS188 4.5 35.5 1.0 NE2 D:HIS211 4.5 42.4 1.0 CD2 D:HIS211 4.5 41.4 1.0 C6 D:TLZ402 4.6 61.5 1.0 O D:HOH525 4.8 31.6 1.0 CA D:ASP185 4.9 39.8 1.0 O6 D:TLZ402 5.0 59.0 1.0

H.Yoshida, A.Yoshihara, T.Ishii, K.Izumori, S.Kamitori. X-Ray Structures of the Pseudomonas Cichorii D-Tagatose 3-Epimerase Mutant Form C66S Recognizing Deoxy Sugars As Substrates Appl. Microbiol. Biotechnol. V. 100 10403 2016.
ISSN: ESSN 1432-0614
PubMed: 27368739
DOI: 10.1007/S00253-016-7673-7