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Chlorine in PDB 6i4d: Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State

Protein crystallography data

The structure of Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State, PDB code: 6i4d 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) 59.93 / 1.24
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 (%) 13 / 15.5

Other elements in 6i4d:

The structure of Crystal Structure of Plasmodium Falciparum Actin I 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 Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State (pdb code 6i4d). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State, PDB code: 6i4d:

Chlorine binding site 1 out of 1 in 6i4d

Go back to Chlorine Binding Sites List in 6i4d
Chlorine binding site 1 out of 1 in the Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Plasmodium Falciparum Actin I in the Mg-K-Atp/Adp State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl407

b:21.3
occ:1.00
O A:HOH581 2.6 37.0 1.0
O A:ALA322 2.6 14.8 1.0
HG A:SER324 2.7 17.1 0.7
O A:THR319 2.8 15.8 1.0
O A:HOH900 2.8 35.0 1.0
O A:HOH899 2.8 43.3 1.0
O A:THR320 3.0 17.6 1.0
OG A:SER324 3.1 14.2 0.7
HA A:THR320 3.4 19.9 1.0
C A:THR320 3.6 16.1 1.0
O A:HOH726 3.8 18.4 1.0
HA A:SER324 3.8 18.7 0.3
HB3 A:SER324 3.8 19.3 0.3
C A:ALA322 3.8 14.7 1.0
HA A:SER324 3.8 16.9 0.7
C A:THR319 3.9 14.8 1.0
CA A:THR320 4.0 16.6 1.0
N A:SER324 4.0 14.4 0.7
N A:SER324 4.1 15.1 0.3
H A:SER324 4.1 17.3 0.7
H A:SER324 4.2 18.1 0.3
CA A:SER324 4.3 14.1 0.7
CB A:SER324 4.3 14.1 0.7
C A:PRO323 4.3 15.1 1.0
CA A:SER324 4.3 15.6 0.3
H A:ALA322 4.3 16.7 1.0
N A:ALA322 4.3 13.9 1.0
O A:HOH943 4.4 49.2 1.0
O A:HOH520 4.4 21.6 1.0
HA A:PRO323 4.4 19.2 1.0
N A:THR320 4.4 15.6 1.0
HG22 A:THR319 4.5 18.3 1.0
CB A:SER324 4.5 16.1 0.3
C A:LEU321 4.5 14.6 1.0
N A:LEU321 4.6 14.9 1.0
O A:HOH803 4.6 30.9 0.5
CA A:ALA322 4.7 13.8 1.0
CA A:PRO323 4.7 16.0 1.0
O A:HOH891 4.7 17.9 0.5
N A:PRO323 4.7 15.6 1.0
O A:PRO323 4.8 15.9 1.0
HB3 A:SER324 4.8 16.9 0.7
HB2 A:SER324 4.8 16.9 0.7
HB3 A:ALA322 4.9 17.9 1.0
O A:LEU321 4.9 16.1 1.0
HG23 A:THR319 4.9 18.3 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: Sat Jul 12 15:38:38 2025

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