Potassium in PDB 5af2: Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3
Protein crystallography data
The structure of Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3, PDB code: 5af2
was solved by
T.Brandmann,
M.Jinek,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.119 /
1.39
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.290,
74.960,
63.220,
90.00,
112.80,
90.00
|
R / Rfree (%)
|
17.13 /
19.28
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3
(pdb code 5af2). 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 the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3, PDB code: 5af2:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 5af2
Go back to
Potassium Binding Sites List in 5af2
Potassium binding site 1 out
of 2 in the Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3
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 the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1837
b:19.4
occ:1.00
|
O18
|
A:15P1836
|
2.7
|
31.7
|
1.0
|
O19
|
A:15P1836
|
2.8
|
39.6
|
1.0
|
O17
|
A:15P1836
|
2.9
|
22.2
|
1.0
|
O21
|
A:15P1836
|
3.0
|
37.0
|
1.0
|
O22
|
A:15P1836
|
3.0
|
42.9
|
1.0
|
O20
|
A:15P1836
|
3.0
|
45.7
|
1.0
|
O23
|
A:15P1836
|
3.0
|
37.8
|
1.0
|
H372
|
A:15P1836
|
3.4
|
42.3
|
1.0
|
C37
|
A:15P1836
|
3.4
|
35.2
|
1.0
|
H412
|
A:15P1836
|
3.4
|
54.1
|
1.0
|
H401
|
A:15P1836
|
3.4
|
52.6
|
1.0
|
H461
|
A:15P1836
|
3.4
|
50.1
|
1.0
|
C39
|
A:15P1836
|
3.5
|
41.6
|
1.0
|
C40
|
A:15P1836
|
3.5
|
43.9
|
1.0
|
H391
|
A:15P1836
|
3.5
|
50.0
|
1.0
|
C41
|
A:15P1836
|
3.5
|
45.1
|
1.0
|
H341
|
A:15P1836
|
3.6
|
31.6
|
1.0
|
C36
|
A:15P1836
|
3.6
|
27.4
|
1.0
|
C46
|
A:15P1836
|
3.6
|
41.8
|
1.0
|
C42
|
A:15P1836
|
3.6
|
40.9
|
1.0
|
H432
|
A:15P1836
|
3.6
|
44.0
|
1.0
|
H421
|
A:15P1836
|
3.7
|
49.0
|
1.0
|
C43
|
A:15P1836
|
3.7
|
36.7
|
1.0
|
C38
|
A:15P1836
|
3.7
|
38.2
|
1.0
|
C35
|
A:15P1836
|
3.7
|
25.9
|
1.0
|
C44
|
A:15P1836
|
3.7
|
40.9
|
1.0
|
H442
|
A:15P1836
|
3.7
|
49.1
|
1.0
|
C34
|
A:15P1836
|
3.8
|
26.3
|
1.0
|
C45
|
A:15P1836
|
3.8
|
44.1
|
1.0
|
H362
|
A:15P1836
|
3.8
|
32.9
|
1.0
|
H322
|
A:15P1836
|
3.9
|
28.5
|
1.0
|
H352
|
A:15P1836
|
3.9
|
31.1
|
1.0
|
H382
|
A:15P1836
|
4.1
|
45.9
|
1.0
|
H452
|
A:15P1836
|
4.1
|
53.0
|
1.0
|
H342
|
A:15P1836
|
4.3
|
31.6
|
1.0
|
H371
|
A:15P1836
|
4.3
|
42.3
|
1.0
|
H392
|
A:15P1836
|
4.4
|
50.0
|
1.0
|
H361
|
A:15P1836
|
4.4
|
32.9
|
1.0
|
H381
|
A:15P1836
|
4.5
|
45.9
|
1.0
|
H402
|
A:15P1836
|
4.5
|
52.6
|
1.0
|
H411
|
A:15P1836
|
4.5
|
54.1
|
1.0
|
H351
|
A:15P1836
|
4.5
|
31.1
|
1.0
|
H462
|
A:15P1836
|
4.5
|
50.1
|
1.0
|
H422
|
A:15P1836
|
4.5
|
49.0
|
1.0
|
H431
|
A:15P1836
|
4.6
|
44.0
|
1.0
|
H441
|
A:15P1836
|
4.6
|
49.1
|
1.0
|
H451
|
A:15P1836
|
4.7
|
53.0
|
1.0
|
C32
|
A:15P1836
|
4.7
|
23.8
|
1.0
|
H321
|
A:15P1836
|
4.9
|
28.5
|
1.0
|
C33
|
A:15P1836
|
5.0
|
25.1
|
1.0
|
|
Potassium binding site 2 out
of 2 in 5af2
Go back to
Potassium Binding Sites List in 5af2
Potassium binding site 2 out
of 2 in the Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3
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 the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1838
b:29.3
occ:1.00
|
O5
|
A:15P1836
|
2.8
|
28.6
|
1.0
|
O4
|
A:15P1836
|
2.8
|
39.7
|
1.0
|
O1
|
A:15P1836
|
2.9
|
49.5
|
1.0
|
OXT
|
A:15P1836
|
2.9
|
49.0
|
1.0
|
O6
|
A:15P1836
|
3.0
|
27.0
|
1.0
|
O2
|
A:15P1836
|
3.0
|
46.4
|
1.0
|
O3
|
A:15P1836
|
3.0
|
50.6
|
1.0
|
H17
|
A:15P1836
|
3.2
|
56.2
|
1.0
|
H21
|
A:15P1836
|
3.3
|
62.6
|
1.0
|
C7
|
A:15P1836
|
3.4
|
46.8
|
1.0
|
C1
|
A:15P1836
|
3.4
|
52.2
|
1.0
|
C8
|
A:15P1836
|
3.5
|
43.4
|
1.0
|
C10
|
A:15P1836
|
3.6
|
35.0
|
1.0
|
H141
|
A:15P1836
|
3.6
|
42.5
|
1.0
|
C2
|
A:15P1836
|
3.6
|
52.9
|
1.0
|
C11
|
A:15P1836
|
3.6
|
25.6
|
1.0
|
H101
|
A:15P1836
|
3.6
|
41.9
|
1.0
|
C3
|
A:15P1836
|
3.6
|
47.1
|
1.0
|
C4
|
A:15P1836
|
3.7
|
44.9
|
1.0
|
C12
|
A:15P1836
|
3.7
|
25.9
|
1.0
|
C5
|
A:15P1836
|
3.7
|
51.7
|
1.0
|
C9
|
A:15P1836
|
3.7
|
39.5
|
1.0
|
H15
|
A:15P1836
|
3.7
|
62.0
|
1.0
|
C6
|
A:15P1836
|
3.7
|
53.5
|
1.0
|
H13
|
A:15P1836
|
3.7
|
56.5
|
1.0
|
H18
|
A:15P1836
|
3.7
|
52.0
|
1.0
|
H14
|
A:15P1836
|
3.7
|
53.9
|
1.0
|
H111
|
A:15P1836
|
3.7
|
30.7
|
1.0
|
HXT
|
A:15P1836
|
3.7
|
58.7
|
1.0
|
H122
|
A:15P1836
|
3.7
|
31.1
|
1.0
|
H12
|
A:15P1836
|
3.8
|
63.5
|
1.0
|
H152
|
A:15P1836
|
3.8
|
33.7
|
1.0
|
H26
|
A:15P1836
|
3.8
|
64.2
|
1.0
|
C13
|
A:15P1836
|
4.0
|
32.6
|
1.0
|
H19
|
A:15P1836
|
4.1
|
47.4
|
1.0
|
H131
|
A:15P1836
|
4.2
|
39.2
|
1.0
|
C14
|
A:15P1836
|
4.3
|
35.4
|
1.0
|
H27
|
A:15P1836
|
4.4
|
56.2
|
1.0
|
H11
|
A:15P1836
|
4.4
|
62.6
|
1.0
|
H28
|
A:15P1836
|
4.4
|
52.0
|
1.0
|
H102
|
A:15P1836
|
4.5
|
41.9
|
1.0
|
H29
|
A:15P1836
|
4.5
|
47.4
|
1.0
|
H112
|
A:15P1836
|
4.5
|
30.7
|
1.0
|
H22
|
A:15P1836
|
4.5
|
63.5
|
1.0
|
H23
|
A:15P1836
|
4.6
|
56.5
|
1.0
|
H24
|
A:15P1836
|
4.6
|
53.9
|
1.0
|
H121
|
A:15P1836
|
4.6
|
31.1
|
1.0
|
H25
|
A:15P1836
|
4.6
|
62.0
|
1.0
|
C15
|
A:15P1836
|
4.6
|
28.1
|
1.0
|
H16
|
A:15P1836
|
4.6
|
64.2
|
1.0
|
H151
|
A:15P1836
|
4.7
|
33.7
|
1.0
|
H132
|
A:15P1836
|
4.8
|
39.2
|
1.0
|
H142
|
A:15P1836
|
5.0
|
42.5
|
1.0
|
|
Reference:
T.Brandmann,
M.Jinek.
Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group A Rotavirus Protein VP3 To Be Published.
Page generated: Mon Aug 12 12:53:50 2024
|