Potassium in PDB 9fq1: Structure of the Disease-Causing Mutant P20S of Human KCTD1

The structure of Structure of the Disease-Causing Mutant P20S of Human KCTD1, PDB code: 9fq1 was solved by N.Balasco, A.Ruggiero, G.Smaldone, L.Esposito, R.Berisio, L.Vitagliano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.99 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.053, 96.003, 116.805, 90, 98.2, 90
R / Rfree (%)	19.4 / 24.3

The binding sites of Potassium atom in the Structure of the Disease-Causing Mutant P20S of Human KCTD1 (pdb code 9fq1). 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 Structure of the Disease-Causing Mutant P20S of Human KCTD1, PDB code: 9fq1:

Potassium binding site 1 out of 1 in the Structure of the Disease-Causing Mutant P20S of Human KCTD1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Disease-Causing Mutant P20S of Human KCTD1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K302 b:70.7 occ:1.00 O A:GLY222 2.6 79.2 1.0 O B:GLY222 2.7 74.4 1.0 O D:GLY222 2.7 73.1 1.0 O C:GLY222 2.7 71.8 1.0 O E:GLY222 2.9 73.2 1.0 O4 C:PO4301 3.2 73.0 1.0 O2 C:PO4301 3.4 81.8 1.0 O1 C:PO4301 3.5 69.3 1.0 C A:GLY222 3.5 79.5 1.0 P C:PO4301 3.6 73.5 1.0 C C:GLY222 3.6 80.6 1.0 C D:GLY222 3.7 76.2 1.0 C B:GLY222 3.7 72.8 1.0 O B:HOH317 3.8 51.1 1.0 C E:GLY222 3.8 80.7 1.0 CA A:GLY223 4.0 82.5 1.0 N A:GLY223 4.1 84.7 1.0 CA C:GLY223 4.1 87.1 1.0 CA B:GLY223 4.2 81.0 1.0 N C:GLY223 4.3 79.2 1.0 CA D:GLY223 4.3 82.4 1.0 CA E:GLY223 4.3 89.2 1.0 N B:GLY223 4.4 73.2 1.0 N D:GLY223 4.4 74.5 1.0 N D:GLY222 4.4 66.8 1.0 N A:GLY222 4.4 79.9 1.0 N E:GLY223 4.5 78.9 1.0 N C:GLY222 4.5 69.2 1.0 CA A:GLY222 4.5 83.3 1.0 N E:GLY222 4.6 70.5 1.0 CA D:GLY222 4.6 74.7 1.0 CA C:GLY222 4.6 77.3 1.0 N B:GLY222 4.6 69.4 1.0 CA B:GLY222 4.8 69.8 1.0 CA E:GLY222 4.8 85.0 1.0

N.Balasco, A.Ruggiero, G.Smaldone, G.Pecoraro, L.Coppola, L.Pirone, E.M.Pedone, L.Esposito, R.Berisio, L.Vitagliano. Structural Studies of KCTD1 and Its Disease-Causing Mutant P20S Provide Insights Into the Protein Function and Misfunction. Int.J.Biol.Macromol. V. 277 34390 2024.
ISSN: ISSN 0141-8130
PubMed: 39111466
DOI: 10.1016/J.IJBIOMAC.2024.134390