Sodium in PDB 6i4f: Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State

The structure of Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State, PDB code: 6i4f 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)	45.18 / 1.50
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	68.760, 71.450, 110.040, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 19.2

The structure of Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Potassium	(K)	1 atom
Calcium	(Ca)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Sodium atom in the Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State (pdb code 6i4f). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State, PDB code: 6i4f:

Sodium binding site 1 out of 1 in the Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Plasmodium Falciparum Actin I (A272W Mutant) in the Mg-K-Atp/Adp State within 5.0Å range: probe atom residue distance (Å) B Occ A:Na407 b:33.4 occ:1.00 HG3 A:LYS292 2.5 64.3 1.0 H A:LYS327 2.5 31.9 1.0 O A:HOH838 2.5 42.0 1.0 O A:LYS327 2.6 25.1 1.0 HB2 A:LYS327 2.6 34.4 1.0 O A:LYS292 2.7 19.3 1.0 HG2 A:LYS292 3.2 64.3 1.0 N A:LYS327 3.3 26.6 1.0 CG A:LYS292 3.3 53.6 1.0 HA A:LYS292 3.3 27.1 1.0 HB2 A:TYR295 3.3 21.5 1.0 H A:GLY296 3.4 22.3 1.0 HA3 A:GLY296 3.4 22.5 1.0 CB A:LYS327 3.4 28.7 1.0 C A:LYS327 3.4 22.6 1.0 N A:GLY296 3.5 18.6 1.0 CA A:LYS327 3.6 25.6 1.0 C A:LYS292 3.6 20.4 1.0 HB3 A:TYR295 3.7 21.5 1.0 HA2 A:GLY296 3.8 22.5 1.0 HE3 A:LYS292 3.8 94.1 1.0 CA A:GLY296 3.8 18.7 1.0 CA A:LYS292 3.8 22.6 1.0 CB A:TYR295 4.0 17.9 1.0 HB3 A:LYS327 4.0 34.4 1.0 CB A:LYS292 4.1 29.8 1.0 C A:TYR295 4.1 16.1 1.0 HA A:MET326 4.2 33.0 1.0 HE2 A:LYS292 4.2 94.1 1.0 HB3 A:MET326 4.3 35.5 1.0 CE A:LYS292 4.3 78.4 1.0 CD A:LYS292 4.4 76.9 1.0 C A:MET326 4.4 24.2 1.0 HD2 A:LYS327 4.4 71.0 1.0 HG3 A:LYS327 4.5 48.7 1.0 HB2 A:LYS292 4.5 35.8 1.0 HA A:LYS327 4.5 30.7 1.0 CG A:LYS327 4.5 40.6 1.0 CA A:TYR295 4.6 19.2 1.0 N A:ILE328 4.7 25.6 1.0 H A:TYR295 4.7 23.2 1.0 CA A:MET326 4.7 27.5 1.0 O A:TYR295 4.8 17.7 1.0 N A:ASP293 4.8 19.5 1.0 HD2 A:LYS292 4.8 92.3 1.0 HB3 A:LYS292 4.9 35.8 1.0 HA A:ILE328 4.9 25.8 1.0 SD A:MET326 4.9 36.1 1.0 N A:TYR295 4.9 19.3 1.0 CD A:LYS327 5.0 59.1 1.0 HD2 A:TYR295 5.0 22.8 1.0 HA A:ASP293 5.0 24.6 1.0 CB A:MET326 5.0 29.6 1.0 HD12 A:ILE328 5.0 42.7 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