Magnesium in PDB 8w2h: Human Liver Phosphofructokinase-1 in the T-State Conformation

All present enzymatic activity of Human Liver Phosphofructokinase-1 in the T-State Conformation:
2.7.1.11;

The binding sites of Magnesium atom in the Human Liver Phosphofructokinase-1 in the T-State Conformation (pdb code 8w2h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Human Liver Phosphofructokinase-1 in the T-State Conformation, PDB code: 8w2h:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Human Liver Phosphofructokinase-1 in the T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Liver Phosphofructokinase-1 in the T-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg805 b:39.6 occ:1.00 OD1 A:ASP119 2.0 38.1 1.0 O2G A:ATP803 2.0 37.1 1.0 O2B A:ATP803 2.6 37.1 1.0 H A:ASP119 2.8 38.1 1.0 HA3 A:GLY118 3.3 33.4 1.0 CG A:ASP119 3.3 38.1 1.0 PG A:ATP803 3.3 37.1 1.0 N A:ASP119 3.5 38.1 1.0 H A:GLY120 3.6 35.0 1.0 PB A:ATP803 3.7 37.1 1.0 O3B A:ATP803 3.7 37.1 1.0 O3G A:ATP803 4.0 37.1 1.0 HB3 A:ASP168 4.1 41.8 1.0 OD2 A:ASP119 4.1 38.1 1.0 CA A:GLY118 4.1 33.4 1.0 HB2 A:ASP166 4.2 34.0 1.0 CB A:ASP119 4.2 38.1 1.0 C A:GLY118 4.3 33.4 1.0 HB3 A:ASP119 4.3 38.1 1.0 O1G A:ATP803 4.3 37.1 1.0 N A:GLY120 4.4 35.0 1.0 HA2 A:GLY118 4.4 33.4 1.0 CA A:ASP119 4.4 38.1 1.0 CG A:ASP166 4.5 34.0 1.0 HB2 A:SER164 4.5 31.1 1.0 OD1 A:ASP166 4.5 34.0 1.0 HB2 A:ASP168 4.6 41.8 1.0 O3A A:ATP803 4.7 37.1 1.0 OD2 A:ASP166 4.7 34.0 1.0 O1B A:ATP803 4.7 37.1 1.0 HB3 A:SER164 4.7 31.1 1.0 CB A:ASP166 4.8 34.0 1.0 CB A:ASP168 4.8 41.8 1.0 O2A A:ATP803 4.9 37.1 1.0 C A:ASP119 4.9 38.1 1.0 HB3 A:ASP166 5.0 34.0 1.0 OD2 A:ASP168 5.0 41.8 1.0

Magnesium binding site 2 out of 4 in the Human Liver Phosphofructokinase-1 in the T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Liver Phosphofructokinase-1 in the T-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg805 b:40.4 occ:1.00 OD1 B:ASP119 2.0 37.8 1.0 O2G B:ATP803 2.0 37.0 1.0 O2B B:ATP803 2.6 37.0 1.0 H B:ASP119 2.8 37.8 1.0 CG B:ASP119 3.3 37.8 1.0 HA3 B:GLY118 3.3 32.8 1.0 PG B:ATP803 3.3 37.0 1.0 N B:ASP119 3.5 37.8 1.0 H B:GLY120 3.6 34.6 1.0 PB B:ATP803 3.7 37.0 1.0 O3B B:ATP803 3.8 37.0 1.0 O3G B:ATP803 4.0 37.0 1.0 HB3 B:ASP168 4.1 41.4 1.0 OD2 B:ASP119 4.1 37.8 1.0 CA B:GLY118 4.1 32.8 1.0 CB B:ASP119 4.2 37.8 1.0 HB2 B:ASP166 4.2 33.8 1.0 HB3 B:ASP119 4.3 37.8 1.0 O1G B:ATP803 4.3 37.0 1.0 C B:GLY118 4.3 32.8 1.0 N B:GLY120 4.4 34.6 1.0 CA B:ASP119 4.4 37.8 1.0 HA2 B:GLY118 4.4 32.8 1.0 CG B:ASP166 4.5 33.8 1.0 HB2 B:SER164 4.5 31.0 1.0 OD1 B:ASP166 4.5 33.8 1.0 O3A B:ATP803 4.7 37.0 1.0 OD2 B:ASP166 4.7 33.8 1.0 HB3 B:SER164 4.7 31.0 1.0 O1B B:ATP803 4.7 37.0 1.0 HB2 B:ASP168 4.8 41.4 1.0 CB B:ASP166 4.8 33.8 1.0 CB B:ASP168 4.9 41.4 1.0 O2A B:ATP803 4.9 37.0 1.0 C B:ASP119 4.9 37.8 1.0 OD2 B:ASP168 5.0 41.4 1.0 CB B:SER164 5.0 31.0 1.0

Magnesium binding site 3 out of 4 in the Human Liver Phosphofructokinase-1 in the T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Human Liver Phosphofructokinase-1 in the T-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg805 b:39.5 occ:1.00 OD1 C:ASP119 2.0 37.7 1.0 O2G C:ATP803 2.0 37.1 1.0 O2B C:ATP803 2.6 37.1 1.0 H C:ASP119 2.8 37.7 1.0 CG C:ASP119 3.3 37.7 1.0 PG C:ATP803 3.3 37.1 1.0 HA3 C:GLY118 3.3 33.0 1.0 N C:ASP119 3.5 37.7 1.0 H C:GLY120 3.6 34.7 1.0 PB C:ATP803 3.7 37.1 1.0 O3B C:ATP803 3.8 37.1 1.0 O3G C:ATP803 4.0 37.1 1.0 HB3 C:ASP168 4.0 41.2 1.0 OD2 C:ASP119 4.1 37.7 1.0 CA C:GLY118 4.1 33.0 1.0 HB2 C:ASP166 4.2 33.6 1.0 CB C:ASP119 4.2 37.7 1.0 HB3 C:ASP119 4.3 37.7 1.0 O1G C:ATP803 4.3 37.1 1.0 C C:GLY118 4.3 33.0 1.0 N C:GLY120 4.4 34.7 1.0 CA C:ASP119 4.4 37.7 1.0 CG C:ASP166 4.4 33.6 1.0 HA2 C:GLY118 4.4 33.0 1.0 HB2 C:SER164 4.5 31.1 1.0 OD1 C:ASP166 4.5 33.6 1.0 OD2 C:ASP166 4.5 33.6 1.0 O3A C:ATP803 4.7 37.1 1.0 HB3 C:SER164 4.7 31.1 1.0 O1B C:ATP803 4.7 37.1 1.0 CB C:ASP166 4.8 33.6 1.0 HB2 C:ASP168 4.8 41.2 1.0 CB C:ASP168 4.8 41.2 1.0 OD2 C:ASP168 4.9 41.2 1.0 O2A C:ATP803 4.9 37.1 1.0 C C:ASP119 5.0 37.7 1.0 HB3 C:ASP166 5.0 33.6 1.0 CB C:SER164 5.0 31.1 1.0

Magnesium binding site 4 out of 4 in the Human Liver Phosphofructokinase-1 in the T-State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Human Liver Phosphofructokinase-1 in the T-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg805 b:39.5 occ:1.00 OD1 D:ASP119 2.0 38.6 1.0 O2G D:ATP803 2.0 37.5 1.0 O2B D:ATP803 2.6 37.5 1.0 H D:ASP119 2.8 38.6 1.0 CG D:ASP119 3.3 38.6 1.0 PG D:ATP803 3.3 37.5 1.0 HA3 D:GLY118 3.3 33.7 1.0 N D:ASP119 3.5 38.6 1.0 H D:GLY120 3.6 35.5 1.0 PB D:ATP803 3.7 37.5 1.0 O3B D:ATP803 3.7 37.5 1.0 O3G D:ATP803 4.0 37.5 1.0 HB3 D:ASP168 4.0 42.0 1.0 OD2 D:ASP119 4.1 38.6 1.0 CA D:GLY118 4.1 33.7 1.0 CB D:ASP119 4.2 38.6 1.0 HB2 D:ASP166 4.3 34.0 1.0 HB3 D:ASP119 4.3 38.6 1.0 O1G D:ATP803 4.3 37.5 1.0 C D:GLY118 4.3 33.7 1.0 N D:GLY120 4.4 35.5 1.0 CA D:ASP119 4.4 38.6 1.0 HA2 D:GLY118 4.4 33.7 1.0 HB2 D:SER164 4.5 31.1 1.0 CG D:ASP166 4.5 34.0 1.0 OD1 D:ASP166 4.5 34.0 1.0 O3A D:ATP803 4.7 37.5 1.0 O1B D:ATP803 4.7 37.5 1.0 HB3 D:SER164 4.7 31.1 1.0 OD2 D:ASP166 4.8 34.0 1.0 HB2 D:ASP168 4.8 42.0 1.0 CB D:ASP168 4.8 42.0 1.0 CB D:ASP166 4.9 34.0 1.0 OD2 D:ASP168 4.9 42.0 1.0 O2A D:ATP803 4.9 37.5 1.0 C D:ASP119 5.0 38.6 1.0 CB D:SER164 5.0 31.1 1.0

E.M.Lynch, H.Hansen, L.Salay, M.Cooper, S.Timr, J.M.Kollman, B.A.Webb. Structural Basis For Allosteric Regulation of Human Phosphofructokinase-1 Nat Commun V. 15 7323 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-51808-6