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Potassium in PDB 6i4j: Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-Adp State

Protein crystallography data

The structure of Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-Adp State, PDB code: 6i4j 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) 45.07 / 1.50
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 68.560, 71.350, 109.670, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 19.8

Other elements in 6i4j:

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

Magnesium (Mg) 1 atom
Calcium (Ca) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-Adp State (pdb code 6i4j). 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 Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-Adp State, PDB code: 6i4j:

Potassium binding site 1 out of 1 in 6i4j

Go back to Potassium Binding Sites List in 6i4j
Potassium binding site 1 out of 1 in the Crystal Structure of Plasmodium Falciparum Actin I (F54Y Mutant) in the Mg-Adp 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-Adp State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K407

b:31.1
occ:0.84
O A:ALA322 2.6 21.4 1.0
HG A:SER324 2.7 34.7 0.7
O A:HOH609 2.7 48.7 1.0
O A:THR319 2.7 22.8 1.0
O A:HOH802 2.9 41.2 1.0
O A:THR320 2.9 24.8 1.0
OG A:SER324 3.2 28.9 0.7
HA A:THR320 3.4 29.4 1.0
C A:THR320 3.6 26.6 1.0
C A:ALA322 3.8 20.8 1.0
HA A:SER324 3.8 53.5 0.3
C A:THR319 3.9 21.7 1.0
HB3 A:SER324 3.9 98.2 0.3
O A:HOH705 3.9 25.9 1.0
HA A:SER324 3.9 24.0 0.7
CA A:THR320 3.9 24.5 1.0
N A:SER324 4.1 17.1 0.7
N A:SER324 4.2 60.3 0.3
O A:HOH833 4.2 51.9 1.0
H A:SER324 4.2 20.5 0.7
H A:ALA322 4.2 24.2 1.0
N A:ALA322 4.3 20.1 1.0
H A:SER324 4.3 72.4 0.3
CB A:SER324 4.3 18.8 0.7
C A:PRO323 4.3 22.4 1.0
CA A:SER324 4.3 20.0 0.7
CA A:SER324 4.4 44.6 0.3
N A:THR320 4.4 21.8 1.0
HA A:PRO323 4.4 28.1 1.0
O A:HOH577 4.5 34.2 1.0
C A:LEU321 4.5 22.0 1.0
N A:LEU321 4.5 21.2 1.0
HG22 A:THR319 4.5 25.7 1.0
CB A:SER324 4.6 81.8 0.3
CA A:ALA322 4.7 20.6 1.0
CA A:PRO323 4.7 23.4 1.0
N A:PRO323 4.7 21.1 1.0
O A:PRO323 4.7 21.1 1.0
HB2 A:SER324 4.8 22.6 0.7
O A:LEU321 4.8 26.8 1.0
HG23 A:THR319 4.9 25.7 1.0
HB3 A:SER324 4.9 22.6 0.7
HB3 A:ALA322 5.0 27.9 1.0

Reference:

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
Page generated: Mon Aug 12 16:39:44 2024

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