Potassium in PDB 6pyp: Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant

All present enzymatic activity of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant:
1.1.1.8;

The structure of Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant, PDB code: 6pyp was solved by A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.00 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.330, 76.560, 64.610, 90.00, 96.57, 90.00
R / Rfree (%)	16.7 / 19

The binding sites of Potassium atom in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant (pdb code 6pyp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant, PDB code: 6pyp:

Potassium binding site 1 out of 1 in the Binary Complex of Human Glycerol 3-Phosphate Dehydrogenase, R269A Mutant


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, R269A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:K402 b:29.7 occ:1.00 O B:PHE32 2.7 23.5 1.0 O B:ALA26 2.7 21.8 1.0 O B:LEU29 2.7 25.5 1.0 O B:HOH614 2.8 30.7 1.0 HD3 B:PRO34 3.2 29.8 1.0 O B:ALA27 3.2 22.5 1.0 O B:HOH634 3.2 38.0 1.0 HA B:ALA30 3.4 35.7 1.0 C B:LEU29 3.5 27.8 1.0 HA B:ALA27 3.5 26.3 1.0 C B:ALA27 3.7 25.4 1.0 C B:PHE32 3.8 24.6 1.0 C B:ALA26 3.8 17.9 1.0 HB3 B:PRO34 3.9 29.3 1.0 H B:PHE32 3.9 24.2 1.0 H B:LEU29 4.0 30.3 1.0 CD B:PRO34 4.0 24.8 1.0 CA B:ALA27 4.0 21.9 1.0 CA B:ALA30 4.1 29.7 1.0 N B:LEU29 4.1 25.2 1.0 HB2 B:PHE32 4.1 24.8 1.0 N B:ALA30 4.1 33.3 1.0 N B:PRO34 4.2 21.4 1.0 HA B:PRO34 4.2 24.4 1.0 O B:ALA30 4.3 30.4 1.0 C B:ALA30 4.3 32.1 1.0 N B:ALA27 4.4 18.5 1.0 C B:GLN28 4.4 25.3 1.0 HG3 B:PRO34 4.4 30.4 1.0 N B:GLN28 4.4 27.9 1.0 CA B:LEU29 4.5 26.7 1.0 CB B:PRO34 4.5 24.4 1.0 N B:PHE32 4.5 20.1 1.0 HA B:ASP33 4.6 28.5 1.0 CA B:PRO34 4.6 20.4 1.0 CG B:PRO34 4.6 25.3 1.0 C B:ASP33 4.6 22.2 1.0 CA B:PHE32 4.6 20.3 1.0 HD2 B:PRO34 4.8 29.8 1.0 O B:HOH555 4.8 30.3 1.0 N B:ASP33 4.8 22.6 1.0 CB B:PHE32 4.8 20.6 1.0 O B:GLN28 4.8 21.9 1.0 HA B:ALA26 4.9 26.1 1.0 H B:ALA30 4.9 39.9 1.0 CA B:ASP33 4.9 23.7 1.0 H B:GLN28 4.9 33.6 1.0 CA B:GLN28 5.0 20.1 1.0

A.R.Mhashal, A.Romero-Rivera, L.S.Mydy, J.R.Cristobal, A.M.Gulick, J.P.Richard, S.C.L.Kamerlin. Modeling the Role of A Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed By Glycerol-3-Phosphate Dehydrogenase. Acs Catalysis V. 10 11253 2020.
ISSN: ESSN 2155-5435
PubMed: 33042609
DOI: 10.1021/ACSCATAL.0C02757