Aluminium 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
Potassium	(K)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Aluminium 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 Aluminium atom.
In total only one binding site of Aluminium was determined in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-K-Adp-Alfn State, PDB code: 6i4i:

Aluminium binding site 1 out of 1 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 Aluminium with other atoms in the Al 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:Al402 b:28.4 occ:1.00 AL A:AF3402 0.0 28.4 1.0 F3 A:AF3402 1.6 32.0 1.0 F2 A:AF3402 1.6 33.6 1.0 F1 A:AF3402 1.6 27.9 1.0 O2B A:ADP401 1.9 29.7 1.0 H A:SER15 3.0 28.6 1.0 PB A:ADP401 3.0 25.2 1.0 HA3 A:GLY157 3.0 28.1 1.0 HG A:SER15 3.2 35.2 1.0 O3B A:ADP401 3.2 24.4 1.0 H A:GLY159 3.3 34.6 1.0 H A:ASP158 3.3 32.9 1.0 HB2 A:SER15 3.3 36.7 1.0 HG12 A:VAL160 3.3 36.8 1.0 O A:HOH658 3.3 36.8 1.0 MG A:MG403 3.3 23.9 1.0 K A:K404 3.5 29.0 0.7 OG A:SER15 3.7 29.3 1.0 H A:VAL160 3.7 40.6 1.0 N A:SER15 3.8 23.8 1.0 O3A A:ADP401 3.8 26.7 1.0 O A:HOH567 3.8 34.6 1.0 HA2 A:GLY14 3.9 33.2 1.0 CB A:SER15 3.9 30.6 1.0 N A:ASP158 3.9 27.4 1.0 CA A:GLY157 4.0 23.4 1.0 O A:HOH570 4.1 25.1 1.0 O1B A:ADP401 4.1 24.6 1.0 O A:HOH643 4.1 25.2 1.0 N A:GLY159 4.1 28.8 1.0 CG1 A:VAL160 4.3 30.7 1.0 H A:GLY16 4.4 30.9 1.0 O A:HOH518 4.4 24.4 1.0 C A:GLY157 4.4 25.5 1.0 N A:VAL160 4.4 33.8 1.0 H A:GLY157 4.5 27.5 1.0 CA A:SER15 4.5 25.5 1.0 HA2 A:GLY75 4.5 30.7 1.0 HA2 A:GLY157 4.5 28.1 1.0 O A:VAL160 4.5 31.9 1.0 HG13 A:VAL160 4.5 36.8 1.0 CA A:GLY14 4.6 27.7 1.0 HA3 A:GLY14 4.6 33.2 1.0 HG11 A:VAL160 4.6 36.8 1.0 HB3 A:ASP158 4.6 38.5 1.0 C A:GLY14 4.7 27.2 1.0 N A:GLY157 4.7 22.9 1.0 HA3 A:GLY159 4.7 37.0 1.0 HB3 A:SER15 4.7 36.7 1.0 HA3 A:GLY75 4.8 30.7 1.0 CA A:GLY159 4.9 30.8 1.0 CA A:ASP158 4.9 28.9 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