Potassium in PDB 6i4g: Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp State
Protein crystallography data
The structure of Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp State, PDB code: 6i4g
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)
|
48.80 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
68.610,
110.620,
138.830,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.7 /
25.7
|
Other elements in 6i4g:
The structure of Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp State also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp State
(pdb code 6i4g). 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 (H74Q) in the Mg-K- Atp State, PDB code: 6i4g:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 6i4g
Go back to
Potassium Binding Sites List in 6i4g
Potassium binding site 1 out
of 2 in the Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp 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 (H74Q) in the Mg-K- Atp State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K403
b:37.8
occ:0.91
|
O
|
A:HOH503
|
2.9
|
42.4
|
1.0
|
O2G
|
A:ATP401
|
2.9
|
30.6
|
1.0
|
O
|
A:VAL160
|
2.9
|
30.8
|
1.0
|
H
|
A:GLY157
|
3.0
|
32.1
|
1.0
|
O1G
|
A:ATP401
|
3.1
|
28.8
|
1.0
|
OD1
|
A:ASP155
|
3.2
|
43.0
|
0.8
|
HG13
|
A:VAL160
|
3.3
|
51.5
|
1.0
|
HG12
|
A:VAL160
|
3.3
|
51.5
|
1.0
|
OD1
|
A:ASP155
|
3.3
|
44.5
|
0.2
|
PG
|
A:ATP401
|
3.4
|
28.2
|
1.0
|
N
|
A:GLY157
|
3.5
|
27.1
|
1.0
|
O
|
A:HOH550
|
3.6
|
26.4
|
1.0
|
CG
|
A:ASP155
|
3.6
|
35.5
|
0.8
|
HA3
|
A:GLY157
|
3.6
|
39.5
|
1.0
|
CG1
|
A:VAL160
|
3.7
|
42.8
|
1.0
|
HA
|
A:SER156
|
3.8
|
39.3
|
1.0
|
HB2
|
A:ASP155
|
3.9
|
37.1
|
0.2
|
OD2
|
A:ASP155
|
3.9
|
39.6
|
0.8
|
C
|
A:VAL160
|
3.9
|
32.7
|
1.0
|
O
|
A:HOH510
|
4.0
|
23.0
|
1.0
|
H
|
A:VAL160
|
4.0
|
50.4
|
1.0
|
HA
|
A:SER161
|
4.1
|
35.1
|
1.0
|
O
|
A:ASP155
|
4.1
|
33.5
|
1.0
|
CA
|
A:GLY157
|
4.1
|
32.9
|
1.0
|
MG
|
A:MG402
|
4.1
|
29.2
|
1.0
|
C
|
A:SER156
|
4.2
|
31.9
|
1.0
|
C
|
A:ASP155
|
4.3
|
29.4
|
1.0
|
HB3
|
A:ASP155
|
4.3
|
36.9
|
0.8
|
CG
|
A:ASP155
|
4.3
|
35.2
|
0.2
|
CA
|
A:SER156
|
4.3
|
32.7
|
1.0
|
HG11
|
A:VAL160
|
4.3
|
51.5
|
1.0
|
N
|
A:SER156
|
4.4
|
30.4
|
1.0
|
CB
|
A:ASP155
|
4.5
|
30.7
|
0.8
|
CB
|
A:ASP155
|
4.5
|
30.8
|
0.2
|
O3G
|
A:ATP401
|
4.6
|
28.1
|
1.0
|
N
|
A:VAL160
|
4.7
|
41.9
|
1.0
|
CA
|
A:VAL160
|
4.7
|
36.2
|
1.0
|
N
|
A:SER161
|
4.8
|
28.3
|
1.0
|
O3B
|
A:ATP401
|
4.8
|
26.1
|
1.0
|
HA2
|
A:GLY157
|
4.8
|
39.5
|
1.0
|
H
|
A:SER156
|
4.8
|
36.5
|
1.0
|
CA
|
A:SER161
|
4.8
|
29.2
|
1.0
|
CB
|
A:VAL160
|
4.9
|
35.1
|
1.0
|
OE1
|
A:GLN138
|
4.9
|
35.0
|
1.0
|
O
|
A:HOH514
|
4.9
|
37.8
|
1.0
|
H
|
A:HIS162
|
5.0
|
33.6
|
1.0
|
|
Potassium binding site 2 out
of 2 in 6i4g
Go back to
Potassium Binding Sites List in 6i4g
Potassium binding site 2 out
of 2 in the Crystal Structure of Plasmodium Falciparum Actin I (H74Q) in the Mg-K- Atp 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 (H74Q) in the Mg-K- Atp State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K403
b:23.1
occ:0.69
|
H
|
B:GLY157
|
2.9
|
29.0
|
1.0
|
O
|
B:VAL160
|
2.9
|
21.6
|
1.0
|
O
|
B:HOH515
|
3.0
|
28.6
|
1.0
|
O2G
|
B:ATP401
|
3.1
|
24.1
|
1.0
|
O
|
B:HOH577
|
3.2
|
38.0
|
1.0
|
O1G
|
B:ATP401
|
3.2
|
24.1
|
1.0
|
HG13
|
B:VAL160
|
3.4
|
36.5
|
1.0
|
N
|
B:GLY157
|
3.4
|
24.1
|
1.0
|
O
|
B:HOH518
|
3.5
|
20.4
|
1.0
|
HA3
|
B:GLY157
|
3.5
|
28.6
|
1.0
|
OD1
|
B:ASP155
|
3.5
|
65.6
|
1.0
|
HG12
|
B:VAL160
|
3.6
|
36.5
|
1.0
|
PG
|
B:ATP401
|
3.6
|
23.6
|
1.0
|
CG
|
B:ASP155
|
3.6
|
58.3
|
1.0
|
OD2
|
B:ASP155
|
3.6
|
62.6
|
1.0
|
O
|
B:HOH513
|
3.7
|
17.8
|
1.0
|
HA
|
B:SER156
|
3.8
|
32.1
|
1.0
|
O
|
B:ASP155
|
3.9
|
28.8
|
1.0
|
C
|
B:VAL160
|
3.9
|
25.9
|
1.0
|
CG1
|
B:VAL160
|
3.9
|
30.3
|
1.0
|
HA
|
B:SER161
|
4.0
|
36.9
|
1.0
|
CA
|
B:GLY157
|
4.0
|
23.8
|
1.0
|
MG
|
B:MG402
|
4.0
|
22.3
|
1.0
|
H
|
B:VAL160
|
4.1
|
40.6
|
1.0
|
C
|
B:SER156
|
4.1
|
25.0
|
1.0
|
C
|
B:ASP155
|
4.1
|
29.4
|
1.0
|
HB3
|
B:ASP155
|
4.2
|
48.0
|
1.0
|
CA
|
B:SER156
|
4.3
|
26.7
|
1.0
|
N
|
B:SER156
|
4.3
|
27.2
|
1.0
|
CB
|
B:ASP155
|
4.5
|
40.0
|
1.0
|
HG11
|
B:VAL160
|
4.5
|
36.5
|
1.0
|
HA2
|
B:GLY157
|
4.6
|
28.6
|
1.0
|
O3G
|
B:ATP401
|
4.6
|
24.6
|
1.0
|
N
|
B:SER161
|
4.7
|
28.4
|
1.0
|
CA
|
B:SER161
|
4.8
|
30.7
|
1.0
|
O
|
B:HOH556
|
4.8
|
29.7
|
1.0
|
N
|
B:VAL160
|
4.8
|
33.8
|
1.0
|
CA
|
B:VAL160
|
4.8
|
30.9
|
1.0
|
H
|
B:SER156
|
4.8
|
32.7
|
1.0
|
OE1
|
B:GLN138
|
4.9
|
30.8
|
1.0
|
H
|
B:HIS162
|
4.9
|
30.6
|
1.0
|
CA
|
B:ASP155
|
5.0
|
32.0
|
1.0
|
C
|
B:GLY157
|
5.0
|
29.6
|
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 16:38:30 2024
|