Potassium in PDB 6i4i: Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State

The structure of Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State, PDB code: 6i4i was solved by E.-P.Kumpula, A.J.Lopez, L.Tajedin, H.Han, I.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.05 / 1.90
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	68.610, 71.330, 109.250, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.7

The structure of Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Magnesium	(Mg)	1 atom
Aluminium	(Al)	1 atom
Calcium	(Ca)	2 atoms

The binding sites of Potassium atom in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State (pdb code 6i4i). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State, PDB code: 6i4i:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State within 5.0Å range: probe atom residue distance (Å) B Occ A:K404 b:29.0 occ:0.74 O A:HOH552 2.8 30.1 1.0 F1 A:AF3402 2.8 27.9 1.0 O A:VAL160 2.8 31.9 1.0 OD1 A:ASP155 2.9 38.6 1.0 H A:GLY157 3.0 27.5 1.0 HG13 A:VAL160 3.1 36.8 1.0 HA3 A:GLY157 3.3 28.1 1.0 F3 A:AF3402 3.3 32.0 1.0 HG12 A:VAL160 3.3 36.8 1.0 O A:HOH518 3.3 24.4 1.0 N A:GLY157 3.4 22.9 1.0 CG A:ASP155 3.4 35.2 1.0 AL A:AF3402 3.5 28.4 1.0 O A:HOH567 3.5 34.6 1.0 O A:HOH570 3.6 25.1 1.0 O A:ASP155 3.6 30.8 1.0 CG1 A:VAL160 3.7 30.7 1.0 C A:VAL160 3.8 30.5 1.0 CA A:GLY157 3.8 23.4 1.0 OD2 A:ASP155 3.9 35.2 1.0 HA A:SER161 3.9 26.1 1.0 HA A:SER156 3.9 31.9 1.0 HB3 A:ASP155 4.0 33.6 1.0 C A:ASP155 4.0 28.6 1.0 MG A:MG403 4.0 23.9 1.0 H A:VAL160 4.1 40.6 1.0 C A:SER156 4.1 25.6 1.0 HD1 A:HIS162 4.2 33.5 1.0 HG11 A:VAL160 4.3 36.8 1.0 CB A:ASP155 4.3 28.0 1.0 CA A:SER156 4.4 26.6 1.0 N A:SER156 4.4 24.7 1.0 HA2 A:GLY157 4.4 28.1 1.0 F2 A:AF3402 4.6 33.6 1.0 N A:SER161 4.6 23.9 1.0 CA A:VAL160 4.6 31.1 1.0 CA A:SER161 4.6 21.8 1.0 H A:HIS162 4.7 31.2 1.0 N A:VAL160 4.7 33.8 1.0 CB A:VAL160 4.8 32.1 1.0 CA A:ASP155 4.8 25.8 1.0 OE1 A:GLN138 4.8 28.2 1.0 O A:HOH608 4.9 30.5 1.0 O2B A:ADP401 4.9 29.7 1.0 H A:SER156 4.9 29.7 1.0 C A:GLY157 5.0 25.5 1.0 ND1 A:HIS162 5.0 27.9 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State within 5.0Å range: probe atom residue distance (Å) B Occ A:K406 b:51.4 occ:1.00 O A:ALA322 2.7 32.4 1.0 O A:THR319 2.7 33.8 1.0 O A:THR320 3.0 32.9 1.0 OG A:SER324 3.3 46.2 1.0 HA A:THR320 3.5 38.5 1.0 C A:THR320 3.6 32.5 1.0 HG A:SER324 3.7 55.5 1.0 O A:HOH609 3.8 46.8 1.0 C A:THR319 3.9 33.2 1.0 C A:ALA322 3.9 32.7 1.0 HA A:SER324 3.9 45.7 1.0 CA A:THR320 4.0 32.1 1.0 N A:SER324 4.2 35.8 1.0 H A:SER324 4.3 43.0 1.0 H A:ALA322 4.3 38.7 1.0 N A:ALA322 4.3 32.2 1.0 O A:HOH537 4.3 44.7 1.0 CA A:SER324 4.4 38.1 1.0 C A:PRO323 4.4 34.6 1.0 N A:THR320 4.4 32.1 1.0 CB A:SER324 4.4 44.1 1.0 HA A:PRO323 4.5 45.8 1.0 C A:LEU321 4.5 35.5 1.0 HG22 A:THR319 4.5 42.8 1.0 N A:LEU321 4.5 36.0 1.0 HG23 A:THR319 4.6 42.8 1.0 CA A:ALA322 4.7 31.0 1.0 CA A:PRO323 4.8 38.2 1.0 O A:PRO323 4.8 30.4 1.0 N A:PRO323 4.8 37.6 1.0 O A:LEU321 4.8 34.2 1.0 HB2 A:SER324 5.0 52.9 1.0

E.P.Kumpula, A.J.Lopez, L.Tajedin, H.Han, I.Kursula. Atomic View Into Plasmodium Actin Polymerization, Atp Hydrolysis, and Fragmentation. Plos Biol. V. 17 00315 2019.
ISSN: ESSN 1545-7885
PubMed: 31199804
DOI: 10.1371/JOURNAL.PBIO.3000315