Potassium in PDB 6e8z: Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad

All present enzymatic activity of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad:
1.1.1.8;

The structure of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad, PDB code: 6e8z was solved by L.S.Mydy, A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.96 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.580, 78.780, 69.179, 90.00, 104.32, 90.00
R / Rfree (%)	16.9 / 22.5

The binding sites of Potassium atom in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad (pdb code 6e8z). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad, PDB code: 6e8z:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad within 5.0Å range: probe atom residue distance (Å) B Occ A:K406 b:44.0 occ:1.00 HD3 A:PRO34 2.6 49.4 1.0 O A:LEU29 2.6 45.9 1.0 O A:ALA26 2.6 35.5 1.0 O A:PHE32 2.8 50.9 1.0 O A:ALA27 3.2 38.2 1.0 CD A:PRO34 3.6 41.2 1.0 HA A:ALA30 3.6 55.8 1.0 C A:LEU29 3.7 43.5 1.0 HA A:ALA27 3.7 41.8 1.0 C A:ALA27 3.7 41.0 1.0 HB3 A:PRO34 3.8 36.3 1.0 C A:ALA26 3.8 46.5 1.0 C A:PHE32 3.9 50.8 1.0 H A:PHE32 4.0 43.4 1.0 N A:PRO34 4.1 37.9 1.0 H A:LEU29 4.1 47.1 1.0 CA A:ALA27 4.1 34.9 1.0 HD2 A:PRO34 4.1 49.4 1.0 N A:LEU29 4.2 39.3 1.0 HA A:PRO34 4.2 36.3 1.0 HG3 A:PRO34 4.3 53.7 1.0 CA A:ALA30 4.3 46.5 1.0 CG A:PRO34 4.3 44.8 1.0 HB2 A:PHE32 4.4 49.5 1.0 CB A:PRO34 4.4 30.3 1.0 N A:ALA30 4.5 40.0 1.0 HA A:ASP33 4.5 40.6 1.0 N A:GLN28 4.5 47.4 1.0 C A:GLN28 4.5 32.7 1.0 CA A:PRO34 4.5 30.3 1.0 N A:ALA27 4.5 41.0 1.0 C A:ALA30 4.5 57.4 1.0 O A:ALA30 4.5 50.6 1.0 CA A:LEU29 4.6 39.0 1.0 C A:ASP33 4.6 37.1 1.0 N A:PHE32 4.7 36.2 1.0 CA A:PHE32 4.8 37.5 1.0 HA A:ALA26 4.8 54.8 1.0 N A:ASP33 4.9 36.4 1.0 CA A:ASP33 4.9 33.8 1.0 O A:GLN28 4.9 35.3 1.0 H A:GLN28 5.0 56.9 1.0 CA A:ALA26 5.0 45.7 1.0

Potassium binding site 2 out of 2 in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase with Nad within 5.0Å range: probe atom residue distance (Å) B Occ B:K404 b:34.5 occ:1.00 O B:LEU29 2.5 39.2 1.0 O B:PHE32 2.7 25.4 1.0 O B:ALA26 2.7 38.0 1.0 O B:HOH584 2.8 42.7 1.0 O B:ALA27 3.0 33.0 1.0 HA B:ALA30 3.3 53.2 1.0 HD3 B:PRO34 3.3 44.5 1.0 O B:HOH598 3.4 48.6 1.0 C B:LEU29 3.5 24.7 1.0 C B:ALA27 3.6 36.5 1.0 HA B:ALA27 3.6 31.7 1.0 C B:PHE32 3.8 34.4 1.0 H B:PHE32 3.8 34.2 1.0 C B:ALA26 3.8 28.8 1.0 H B:LEU29 4.0 35.8 1.0 HB3 B:PRO34 4.1 40.8 1.0 CA B:ALA30 4.1 44.4 1.0 CA B:ALA27 4.1 26.4 1.0 HB2 B:PHE32 4.1 36.6 1.0 N B:LEU29 4.1 29.8 1.0 CD B:PRO34 4.2 37.1 1.0 N B:ALA30 4.2 33.9 1.0 N B:PRO34 4.3 34.5 1.0 HA B:PRO34 4.3 30.3 1.0 N B:ALA27 4.4 29.4 1.0 CA B:LEU29 4.4 27.9 1.0 C B:GLN28 4.4 31.6 1.0 C B:ALA30 4.5 36.5 1.0 N B:PHE32 4.5 28.6 1.0 N B:GLN28 4.5 32.2 1.0 HA B:ASP33 4.5 39.7 1.0 CA B:PHE32 4.6 33.5 1.0 C B:ASP33 4.6 32.3 1.0 O B:ALA30 4.6 41.0 1.0 CA B:PRO34 4.7 25.3 1.0 CB B:PRO34 4.7 34.0 1.0 N B:ASP33 4.8 28.6 1.0 CB B:PHE32 4.8 30.5 1.0 HD2 B:PRO34 4.8 44.5 1.0 HA B:ALA26 4.8 44.7 1.0 O B:GLN28 4.9 26.2 1.0 O B:HOH567 4.9 41.8 1.0 CA B:ASP33 4.9 33.1 1.0 HG3 B:PRO34 4.9 41.0 1.0 CG B:PRO34 4.9 34.2 1.0 H B:ALA30 5.0 40.6 1.0 CA B:GLN28 5.0 25.1 1.0

L.S.Mydy, J.R.Cristobal, R.D.Katigbak, P.Bauer, A.C.Reyes, S.C.L.Kamerlin, J.P.Richard, A.M.Gulick. Human Glycerol 3-Phosphate Dehydrogenase: X-Ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies. Biochemistry V. 58 1061 2019.
ISSN: ISSN 1520-4995
PubMed: 30640445
DOI: 10.1021/ACS.BIOCHEM.8B01103