Magnesium in PDB 6ls5: Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor

The structure of Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor, PDB code: 6ls5 was solved by H.Yunyuan, S.Rongrong, X.Yixiang, N.Shuaishuai, R.Yanliang, L.Jian, W.Jian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.84 / 2.03
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.599, 83.523, 276.929, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.7

The binding sites of Magnesium atom in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor (pdb code 6ls5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor, PDB code: 6ls5:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:19.3 occ:1.00 OE2 A:GLU98 2.2 34.9 1.0 O A:LEU120 2.2 30.1 1.0 OE1 A:GLU97 2.4 30.1 1.0 O A:HOH605 2.4 32.9 1.0 O A:HOH571 2.4 30.5 1.0 OD1 A:ASP118 2.5 24.7 1.0 CD A:GLU97 3.4 32.3 1.0 CD A:GLU98 3.4 34.4 1.0 CG A:ASP118 3.4 26.9 1.0 C A:LEU120 3.4 29.8 1.0 OD2 A:ASP118 3.7 29.5 1.0 CA A:ASP121 4.0 27.1 1.0 OE2 A:GLU97 4.1 37.6 1.0 CG A:GLU97 4.2 27.3 1.0 OE1 A:GLU98 4.2 34.7 1.0 N A:ASP121 4.2 25.2 1.0 CB A:GLU97 4.2 26.2 1.0 CG A:GLU98 4.3 27.4 1.0 N A:LEU120 4.3 23.6 1.0 OD2 A:ASP74 4.5 38.6 1.0 CA A:LEU120 4.5 25.4 1.0 CD A:PRO119 4.5 23.9 1.0 O A:HOH508 4.7 38.8 1.0 OG A:SER124 4.7 43.7 1.0 CB A:ASP118 4.7 23.5 1.0 CG A:ASP74 4.8 37.8 1.0 O A:HOH608 4.8 40.5 1.0 CB A:ASP121 4.8 29.5 1.0 N A:PRO119 4.9 19.1 1.0

Magnesium binding site 2 out of 4 in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:26.7 occ:1.00 OE1 B:GLU98 2.2 34.1 1.0 OE1 B:GLU97 2.3 38.8 1.0 OD1 B:ASP118 2.4 30.8 1.0 O B:HOH525 2.4 31.6 1.0 O B:HOH603 2.5 32.5 1.0 O B:LEU120 3.0 32.2 1.0 CG B:ASP118 3.4 26.4 1.0 CD B:GLU97 3.4 34.4 1.0 CD B:GLU98 3.4 36.0 1.0 OD2 B:ASP118 3.7 34.4 1.0 C B:LEU120 3.7 31.7 1.0 CB B:GLU97 4.1 28.5 1.0 OE2 B:GLU98 4.2 35.0 1.0 CG B:GLU97 4.2 32.3 1.0 N B:LEU120 4.3 24.3 1.0 OE2 B:GLU97 4.3 37.6 1.0 CG B:GLU98 4.4 31.5 1.0 N B:ASP121 4.4 37.0 1.0 CA B:ASP121 4.5 40.8 1.0 CD B:PRO119 4.5 24.2 1.0 CA B:LEU120 4.6 26.7 1.0 CB B:ASP118 4.7 23.5 1.0 OG B:SER123 4.8 57.2 1.0 O B:HOH614 4.8 43.0 1.0 N B:PRO119 4.9 23.6 1.0 CB B:SER123 4.9 53.2 1.0 CG B:PRO119 5.0 19.7 1.0

Magnesium binding site 3 out of 4 in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg402 b:45.3 occ:1.00 OD2 C:ASP118 2.2 37.5 1.0 OE2 C:GLU97 2.2 44.8 1.0 OE2 C:GLU280 2.3 42.3 1.0 OD1 C:ASP121 2.7 36.8 1.0 CD C:GLU97 3.1 44.0 1.0 CG C:ASP118 3.2 32.6 1.0 OE1 C:GLU97 3.4 51.6 1.0 CD C:GLU280 3.5 32.7 1.0 CG C:ASP121 3.7 40.1 1.0 OD1 C:ASP118 3.7 33.6 1.0 O C:HOH564 3.9 39.5 1.0 CB C:ASP121 3.9 33.4 1.0 CA C:ASP121 4.0 31.6 1.0 OE1 C:GLU280 4.3 36.5 1.0 CG C:GLU280 4.4 32.2 1.0 CB C:ASP118 4.5 28.7 1.0 CG C:GLU97 4.5 36.1 1.0 O C:HOH643 4.6 42.4 1.0 N C:GLY122 4.8 39.1 1.0 OD2 C:ASP121 4.8 42.8 1.0 N C:ASP121 4.9 30.4 1.0 C C:ASP121 5.0 32.7 1.0

Magnesium binding site 4 out of 4 in the Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Human Liver Fbpase Complexed with Covalent Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg402 b:41.6 occ:1.00 O D:HOH599 2.1 45.9 1.0 OD1 D:ASP121 2.2 37.9 1.0 OE1 D:GLU97 2.2 48.0 1.0 OE2 D:GLU280 2.4 37.6 1.0 OD2 D:ASP118 2.5 39.2 1.0 O D:HOH592 3.0 45.4 1.0 CD D:GLU97 3.2 47.6 1.0 CG D:ASP121 3.4 41.2 1.0 OE2 D:GLU97 3.5 54.6 1.0 CG D:ASP118 3.5 35.3 1.0 CD D:GLU280 3.6 32.3 1.0 OD1 D:ASP118 3.8 36.9 1.0 O D:HOH597 3.9 45.0 1.0 CB D:ASP121 4.0 31.8 1.0 CA D:ASP121 4.2 36.4 1.0 CG D:GLU280 4.4 33.1 1.0 OD2 D:ASP121 4.4 41.9 1.0 OE1 D:GLU280 4.4 30.3 1.0 CG D:GLU97 4.6 43.8 1.0 CB D:ASP118 4.8 29.5 1.0 N D:GLY122 4.9 36.2 1.0

Y.Huang, Y.Xu, R.Song, S.Ni, J.Liu, Y.Xu, Y.Ren, L.Rao, Y.Wang, L.Wei, L.Feng, C.Su, C.Peng, J.Li, J.Wan. Identification of the New Covalent Allosteric Binding Site of Fbpase with Disulfiram Derivatives Toward Glucose Reduction. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32375478
DOI: 10.1021/ACS.JMEDCHEM.0C00699