Manganese in PDB 8g5x: Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate

The structure of Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate, PDB code: 8g5x was solved by C.Abad-Zapatero, A.I.Selezneva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.18 / 2.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	63.76, 74.577, 77.191, 67.89, 67.89, 77.01
R / Rfree (%)	16.5 / 22.7

The binding sites of Manganese atom in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate (pdb code 8g5x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate, PDB code: 8g5x:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate


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 Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:130.6 occ:1.00 O A:LEU86 2.2 56.5 1.0 O A:HOH568 2.3 85.4 1.0 OD1 A:ASP84 2.3 72.8 1.0 H A:LEU86 2.8 48.3 1.0 C A:LEU86 2.8 50.2 1.0 HA A:GLU87 3.3 61.6 1.0 CG A:ASP84 3.4 57.2 1.0 N A:GLU87 3.5 52.5 1.0 N A:LEU86 3.5 40.2 1.0 O A:HOH516 3.5 70.8 1.0 CA A:LEU86 3.7 41.1 1.0 HD2 A:PRO85 3.8 59.6 1.0 CA A:GLU87 3.9 51.3 1.0 OD2 A:ASP84 3.9 55.2 1.0 HB3 A:LEU86 3.9 49.1 1.0 H A:GLY88 4.1 67.1 1.0 H A:GLU87 4.1 63.1 1.0 HA A:ASP84 4.2 51.7 1.0 OE2 A:GLU57 4.3 88.5 1.0 CB A:LEU86 4.4 40.9 1.0 OD2 A:ASP33 4.4 64.2 1.0 N A:PRO85 4.5 52.7 1.0 HA A:LEU86 4.5 49.3 1.0 C A:ASP84 4.5 47.9 1.0 N A:GLY88 4.5 55.9 1.0 CB A:ASP84 4.5 54.1 1.0 CD A:PRO85 4.6 49.6 1.0 C A:GLU87 4.6 55.5 1.0 CA A:ASP84 4.6 43.0 1.0 C A:PRO85 4.7 41.1 1.0 HB2 A:GLU87 4.8 61.6 1.0 HG A:LEU86 4.8 43.0 1.0 O A:GLY88 4.9 60.8 1.0 HB3 A:ASP84 4.9 65.0 1.0

Manganese binding site 2 out of 4 in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate


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 Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn405 b:124.0 occ:1.00 OD1 B:ASP84 2.3 68.2 1.0 O B:HOH502 2.4 100.2 1.0 O B:LEU86 2.6 51.3 1.0 HO1 B:GOL403 3.2 84.1 1.0 O B:HOH514 3.2 50.1 1.0 CG B:ASP84 3.4 55.3 1.0 H B:LEU86 3.5 55.0 1.0 C B:LEU86 3.5 47.2 1.0 O B:HOH596 3.5 74.0 1.0 OD2 B:ASP84 3.8 59.0 1.0 HA B:GLU87 3.9 67.7 1.0 HD2 B:PRO85 3.9 57.2 1.0 HG23 B:THR89 3.9 63.1 1.0 O1 B:GOL403 4.0 70.0 1.0 HA B:ASP84 4.2 57.8 1.0 N B:GLU87 4.2 45.7 1.0 N B:LEU86 4.2 45.9 1.0 OE1 B:GLU57 4.3 72.6 1.0 HG21 B:THR89 4.3 63.1 1.0 OD1 B:ASP33 4.4 75.4 1.0 HG22 B:THR89 4.4 63.1 1.0 CG2 B:THR89 4.5 52.6 1.0 CA B:LEU86 4.5 46.2 1.0 HB3 B:LEU86 4.5 50.6 1.0 CA B:GLU87 4.5 56.4 1.0 H B:GLY88 4.5 58.8 1.0 CB B:ASP84 4.6 53.5 1.0 CD B:PRO85 4.8 47.7 1.0 CA B:ASP84 4.8 48.2 1.0 H B:GLU87 4.8 54.9 1.0 H12 B:GOL403 4.9 98.3 1.0 N B:PRO85 4.9 51.1 1.0 C1 B:GOL403 5.0 81.9 1.0 C B:ASP84 5.0 53.0 1.0

Manganese binding site 3 out of 4 in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn606 b:109.8 occ:1.00 O C:HOH755 2.2 51.6 1.0 O C:LEU86 2.2 42.9 1.0 O C:HOH842 2.2 89.0 1.0 OD1 C:ASP84 2.3 61.0 1.0 H C:LEU86 2.8 49.5 1.0 C C:LEU86 2.9 37.5 1.0 O C:HOH851 3.2 61.0 1.0 CG C:ASP84 3.3 51.8 1.0 N C:LEU86 3.5 41.2 1.0 HA C:GLU87 3.6 52.0 1.0 HD2 C:PRO85 3.6 56.4 1.0 N C:GLU87 3.6 44.6 1.0 HG23 C:THR89 3.6 57.8 1.0 CA C:LEU86 3.7 43.3 1.0 O C:HOH705 3.7 42.7 1.0 OD2 C:ASP84 3.8 49.5 1.0 HB3 C:LEU86 3.9 44.3 1.0 HA C:ASP84 4.0 56.5 1.0 CA C:GLU87 4.1 43.3 1.0 H C:GLU87 4.2 53.6 1.0 H C:GLY88 4.3 45.3 1.0 CG2 C:THR89 4.3 48.1 1.0 CB C:LEU86 4.4 36.9 1.0 HG22 C:THR89 4.4 57.8 1.0 CD C:PRO85 4.4 47.0 1.0 HG21 C:THR89 4.4 57.8 1.0 N C:PRO85 4.4 44.4 1.0 OE1 C:GLU57 4.4 52.2 1.0 C C:ASP84 4.5 45.6 1.0 CB C:ASP84 4.5 44.7 1.0 CA C:ASP84 4.5 47.1 1.0 HA C:LEU86 4.5 52.0 1.0 C C:PRO85 4.7 42.7 1.0 OD1 C:ASP33 4.7 55.0 1.0 HB2 C:PRO85 4.8 56.6 1.0 O C:HOH729 4.8 43.9 1.0 HB3 C:ASP84 4.8 53.7 1.0 O1P C:FBP604 4.8 100.7 1.0 N C:GLY88 4.9 37.7 1.0 HB2 C:GLU87 4.9 50.1 1.0 H C:THR89 4.9 46.9 1.0 HD3 C:PRO85 5.0 56.4 1.0

Manganese binding site 4 out of 4 in the Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of the Class II Fructose-1,6-Bisphophatase From Francisella Tularensis Complexed with Native Metal Cofactor Mn++ and Substrate Fructose-1,6-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn404 b:128.5 occ:1.00 O D:HOH597 2.3 116.6 1.0 O D:HOH594 2.3 107.7 1.0 O D:HOH615 2.5 85.2 1.0 OD1 D:ASP84 2.7 66.5 1.0 HD2 D:PRO85 3.7 80.4 1.0 CG D:ASP84 3.7 64.8 1.0 HA D:ASP84 3.9 81.2 1.0 O D:HOH530 4.0 82.5 1.0 OD2 D:ASP84 4.1 65.8 1.0 O D:LEU86 4.1 77.2 1.0 O D:HOH511 4.5 58.3 1.0 HG23 D:THR89 4.5 87.2 1.0 H D:LEU86 4.6 88.0 1.0 CD D:PRO85 4.6 67.0 1.0 HA D:GLU87 4.7 87.8 1.0 CA D:ASP84 4.7 67.6 1.0 OE2 D:GLU214 4.8 56.3 1.0 CB D:ASP84 4.8 62.7 1.0 HG21 D:THR89 4.9 87.2 1.0 HD3 D:PRO85 4.9 80.4 1.0

A.I.Selezneva, L.N.M.Harding, H.J.Gutka, F.Movahedzadeh, C.Abad-Zapatero. New Structures of Class II Fructose-1,6-Bisphosphatase From Francisella Tularensis Provide A Framework For A Novel Catalytic Mechanism For the Entire Class Plos One 2023.
ISSN: ESSN 1932-6203