Potassium in PDB 4xra: Salmonella Typhimurium Ahpc T43S Mutant
Enzymatic activity of Salmonella Typhimurium Ahpc T43S Mutant
All present enzymatic activity of Salmonella Typhimurium Ahpc T43S Mutant:
1.11.1.15;
Protein crystallography data
The structure of Salmonella Typhimurium Ahpc T43S Mutant, PDB code: 4xra
was solved by
A.Perkins,
A.E.Brereton,
K.Nelson,
D.Parsonage,
L.Poole,
P.A.Karplus,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
36.28 /
1.75
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
127.069,
171.920,
135.290,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.1 /
20
|
Other elements in 4xra:
The structure of Salmonella Typhimurium Ahpc T43S Mutant also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Salmonella Typhimurium Ahpc T43S Mutant
(pdb code 4xra). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the
Salmonella Typhimurium Ahpc T43S Mutant, PDB code: 4xra:
Jump to Potassium binding site number:
1;
2;
3;
Potassium binding site 1 out
of 3 in 4xra
Go back to
Potassium Binding Sites List in 4xra
Potassium binding site 1 out
of 3 in the Salmonella Typhimurium Ahpc T43S Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K204
b:52.0
occ:0.50
|
O
|
A:THR72
|
2.9
|
24.9
|
1.0
|
O
|
A:HOH312
|
2.9
|
28.0
|
1.0
|
O
|
A:HOH306
|
3.1
|
27.5
|
1.0
|
HA
|
A:ASP73
|
3.6
|
30.9
|
1.0
|
HA
|
A:PRO99
|
3.6
|
31.3
|
1.0
|
HB
|
A:THR72
|
3.7
|
31.9
|
1.0
|
C
|
A:THR72
|
3.8
|
23.7
|
1.0
|
HB3
|
A:PRO99
|
3.9
|
32.2
|
1.0
|
OG1
|
A:THR72
|
4.3
|
25.5
|
1.0
|
CB
|
A:THR72
|
4.4
|
26.6
|
1.0
|
CA
|
A:ASP73
|
4.4
|
25.8
|
1.0
|
N
|
A:ASP73
|
4.4
|
25.6
|
1.0
|
HG1
|
A:THR72
|
4.4
|
30.6
|
1.0
|
CA
|
A:PRO99
|
4.5
|
26.1
|
1.0
|
CB
|
A:PRO99
|
4.6
|
26.9
|
1.0
|
O
|
A:PRO99
|
4.8
|
26.5
|
1.0
|
CA
|
A:THR72
|
4.8
|
25.0
|
1.0
|
HB2
|
A:PRO99
|
4.8
|
32.2
|
1.0
|
O
|
A:HOH301
|
4.9
|
29.5
|
1.0
|
HG23
|
A:THR74
|
5.0
|
29.0
|
1.0
|
|
Potassium binding site 2 out
of 3 in 4xra
Go back to
Potassium Binding Sites List in 4xra
Potassium binding site 2 out
of 3 in the Salmonella Typhimurium Ahpc T43S Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K203
b:52.2
occ:1.00
|
O
|
C:THR72
|
2.8
|
26.8
|
1.0
|
O
|
B:THR72
|
2.9
|
24.8
|
1.0
|
O
|
B:HOH345
|
2.9
|
27.7
|
1.0
|
O
|
C:HOH319
|
2.9
|
27.7
|
1.0
|
O
|
B:HOH351
|
3.1
|
29.5
|
1.0
|
O
|
C:HOH322
|
3.1
|
28.4
|
1.0
|
HA
|
C:PRO99
|
3.5
|
28.4
|
1.0
|
HA
|
B:PRO99
|
3.5
|
31.4
|
1.0
|
HA
|
C:ASP73
|
3.6
|
32.2
|
1.0
|
HA
|
B:ASP73
|
3.6
|
27.6
|
1.0
|
C
|
C:THR72
|
3.7
|
27.5
|
1.0
|
HB3
|
C:PRO99
|
3.7
|
29.1
|
1.0
|
HB
|
C:THR72
|
3.8
|
29.6
|
1.0
|
HB
|
B:THR72
|
3.8
|
24.8
|
1.0
|
HB3
|
B:PRO99
|
3.8
|
33.8
|
1.0
|
C
|
B:THR72
|
3.8
|
25.7
|
1.0
|
OG1
|
C:THR72
|
4.3
|
25.3
|
1.0
|
CA
|
C:PRO99
|
4.3
|
23.7
|
1.0
|
CB
|
C:PRO99
|
4.3
|
24.2
|
1.0
|
CA
|
B:PRO99
|
4.4
|
26.1
|
1.0
|
CA
|
C:ASP73
|
4.4
|
26.9
|
1.0
|
CA
|
B:ASP73
|
4.4
|
23.0
|
1.0
|
CB
|
C:THR72
|
4.4
|
24.6
|
1.0
|
OG1
|
B:THR72
|
4.4
|
22.9
|
1.0
|
N
|
C:ASP73
|
4.4
|
24.4
|
1.0
|
HG1
|
C:THR72
|
4.4
|
30.3
|
1.0
|
N
|
B:ASP73
|
4.4
|
25.1
|
1.0
|
CB
|
B:THR72
|
4.4
|
20.6
|
1.0
|
CB
|
B:PRO99
|
4.5
|
28.2
|
1.0
|
HB2
|
C:PRO99
|
4.5
|
29.1
|
1.0
|
HG1
|
B:THR72
|
4.5
|
27.4
|
1.0
|
HB2
|
B:PRO99
|
4.7
|
33.8
|
1.0
|
CA
|
C:THR72
|
4.7
|
24.7
|
1.0
|
O
|
C:PRO99
|
4.8
|
24.8
|
1.0
|
O
|
B:PRO99
|
4.8
|
24.8
|
1.0
|
CA
|
B:THR72
|
4.8
|
24.1
|
1.0
|
HG23
|
C:THR74
|
4.9
|
31.1
|
1.0
|
O
|
B:HOH343
|
4.9
|
30.0
|
1.0
|
HG23
|
B:THR74
|
4.9
|
30.4
|
1.0
|
O
|
C:HOH317
|
4.9
|
28.9
|
1.0
|
|
Potassium binding site 3 out
of 3 in 4xra
Go back to
Potassium Binding Sites List in 4xra
Potassium binding site 3 out
of 3 in the Salmonella Typhimurium Ahpc T43S Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K203
b:60.4
occ:1.00
|
O
|
E:THR72
|
2.8
|
31.4
|
1.0
|
O
|
D:THR72
|
2.8
|
30.2
|
1.0
|
O
|
E:HOH337
|
2.9
|
34.4
|
1.0
|
O
|
D:HOH336
|
2.9
|
33.9
|
1.0
|
O
|
E:HOH336
|
3.0
|
35.1
|
1.0
|
O
|
D:HOH418
|
3.1
|
35.5
|
1.0
|
HA
|
E:PRO99
|
3.5
|
38.1
|
1.0
|
HA
|
E:ASP73
|
3.5
|
39.2
|
1.0
|
HA
|
D:ASP73
|
3.5
|
37.6
|
1.0
|
HA
|
D:PRO99
|
3.6
|
36.9
|
1.0
|
C
|
E:THR72
|
3.8
|
33.3
|
1.0
|
HB
|
D:THR72
|
3.8
|
35.5
|
1.0
|
C
|
D:THR72
|
3.8
|
31.7
|
1.0
|
HB3
|
D:PRO99
|
3.8
|
34.1
|
1.0
|
HB3
|
E:PRO99
|
3.8
|
39.4
|
1.0
|
HB
|
E:THR72
|
3.9
|
36.8
|
1.0
|
OG1
|
E:THR72
|
4.3
|
29.3
|
1.0
|
OG1
|
D:THR72
|
4.3
|
31.5
|
1.0
|
CA
|
E:ASP73
|
4.3
|
32.7
|
1.0
|
CA
|
E:PRO99
|
4.3
|
31.8
|
1.0
|
CA
|
D:ASP73
|
4.4
|
31.4
|
1.0
|
N
|
D:ASP73
|
4.4
|
30.8
|
1.0
|
N
|
E:ASP73
|
4.4
|
30.9
|
1.0
|
CB
|
D:THR72
|
4.4
|
29.6
|
1.0
|
CA
|
D:PRO99
|
4.4
|
30.8
|
1.0
|
HG1
|
D:THR72
|
4.4
|
37.8
|
1.0
|
HG1
|
E:THR72
|
4.4
|
35.2
|
1.0
|
CB
|
D:PRO99
|
4.5
|
28.4
|
1.0
|
CB
|
E:PRO99
|
4.5
|
32.8
|
1.0
|
CB
|
E:THR72
|
4.5
|
30.7
|
1.0
|
HB2
|
D:PRO99
|
4.7
|
34.1
|
1.0
|
HB2
|
E:PRO99
|
4.7
|
39.4
|
1.0
|
CA
|
E:THR72
|
4.8
|
30.0
|
1.0
|
CA
|
D:THR72
|
4.8
|
29.9
|
1.0
|
O
|
E:PRO99
|
4.8
|
32.6
|
1.0
|
O
|
D:PRO99
|
4.8
|
31.5
|
1.0
|
HG23
|
E:THR74
|
4.8
|
39.7
|
1.0
|
O
|
D:HOH333
|
4.9
|
39.5
|
1.0
|
HG23
|
D:THR74
|
4.9
|
39.0
|
1.0
|
O
|
E:HOH332
|
4.9
|
35.9
|
1.0
|
C
|
E:ASP73
|
5.0
|
37.1
|
1.0
|
|
Reference:
K.J.Nelson,
A.Perkins,
A.E.D.Van Swearingen,
S.Hartman,
A.E.Brereton,
D.Parsonage,
F.R.Salsbury Jr.,
P.A.Karplus,
L.B.Poole.
Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxid.Redox Signal. V. 28 521 2018.
ISSN: ESSN 1557-7716
PubMed: 28375740
DOI: 10.1089/ARS.2016.6922
Page generated: Mon Aug 12 12:38:24 2024
|