Sodium in PDB 2wdr: E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
Enzymatic activity of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
All present enzymatic activity of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound:
1.3.5.1;
1.3.99.1;
Protein crystallography data
The structure of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound, PDB code: 2wdr
was solved by
J.Ruprecht,
V.Yankovskaya,
E.Maklashina,
S.Iwata,
G.Cecchini,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.52 /
3.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
119.955,
186.128,
204.034,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.7 /
22.8
|
Other elements in 2wdr:
The structure of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
(pdb code 2wdr). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the
E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound, PDB code: 2wdr:
Jump to Sodium binding site number:
1;
2;
3;
Sodium binding site 1 out
of 3 in 2wdr
Go back to
Sodium Binding Sites List in 2wdr
Sodium binding site 1 out
of 3 in the E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1590
b:2.0
occ:1.00
|
O
|
A:GLY358
|
2.4
|
48.4
|
1.0
|
O
|
A:GLU388
|
2.5
|
48.9
|
1.0
|
O
|
A:MET356
|
2.7
|
48.0
|
1.0
|
O
|
A:ALA390
|
2.7
|
48.7
|
1.0
|
O
|
A:MET357
|
3.0
|
48.0
|
1.0
|
C
|
A:MET357
|
3.4
|
48.0
|
1.0
|
C
|
A:GLU388
|
3.5
|
48.8
|
1.0
|
C
|
A:GLY358
|
3.6
|
48.4
|
1.0
|
C
|
A:ALA390
|
3.7
|
48.5
|
1.0
|
OH
|
A:TYR355
|
3.7
|
48.8
|
1.0
|
C
|
A:MET356
|
3.8
|
48.0
|
1.0
|
N
|
A:GLY358
|
3.9
|
48.3
|
1.0
|
CA
|
A:MET357
|
4.0
|
47.9
|
1.0
|
CA
|
A:GLU388
|
4.0
|
48.8
|
1.0
|
CA
|
A:GLY358
|
4.3
|
48.4
|
1.0
|
N
|
A:ALA390
|
4.3
|
48.6
|
1.0
|
CZ
|
A:TYR355
|
4.3
|
48.6
|
1.0
|
N
|
A:MET357
|
4.4
|
48.0
|
1.0
|
CE2
|
A:TYR355
|
4.4
|
48.4
|
1.0
|
N
|
A:CYS391
|
4.4
|
48.5
|
1.0
|
CA
|
A:CYS391
|
4.5
|
48.5
|
1.0
|
CE
|
A:MET356
|
4.5
|
49.3
|
1.0
|
CG
|
A:GLU388
|
4.5
|
48.8
|
1.0
|
O
|
A:GLY387
|
4.5
|
48.5
|
1.0
|
C
|
A:ILE389
|
4.6
|
48.8
|
1.0
|
N
|
A:GLY359
|
4.6
|
48.2
|
1.0
|
N
|
A:ILE389
|
4.6
|
48.7
|
1.0
|
CA
|
A:ALA390
|
4.6
|
48.6
|
1.0
|
CB
|
A:CYS391
|
4.7
|
48.4
|
1.0
|
CG
|
A:MET356
|
4.8
|
48.4
|
1.0
|
CA
|
A:GLY359
|
4.8
|
48.3
|
1.0
|
CB
|
A:GLU388
|
4.9
|
48.8
|
1.0
|
CA
|
A:ILE389
|
5.0
|
48.6
|
1.0
|
|
Sodium binding site 2 out
of 3 in 2wdr
Go back to
Sodium Binding Sites List in 2wdr
Sodium binding site 2 out
of 3 in the E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Na1590
b:12.1
occ:1.00
|
O
|
E:GLY358
|
2.4
|
48.2
|
1.0
|
O
|
E:ALA390
|
2.6
|
48.6
|
1.0
|
O
|
E:GLU388
|
2.6
|
48.7
|
1.0
|
O
|
E:MET356
|
2.8
|
47.7
|
1.0
|
O
|
E:MET357
|
2.9
|
48.1
|
1.0
|
C
|
E:MET357
|
3.3
|
48.1
|
1.0
|
C
|
E:GLY358
|
3.5
|
48.3
|
1.0
|
C
|
E:ALA390
|
3.6
|
48.4
|
1.0
|
C
|
E:GLU388
|
3.6
|
48.6
|
1.0
|
OH
|
E:TYR355
|
3.8
|
48.7
|
1.0
|
C
|
E:MET356
|
3.9
|
47.9
|
1.0
|
N
|
E:GLY358
|
3.9
|
48.3
|
1.0
|
CA
|
E:MET357
|
4.0
|
47.9
|
1.0
|
CA
|
E:GLU388
|
4.1
|
48.6
|
1.0
|
CA
|
E:GLY358
|
4.2
|
48.3
|
1.0
|
N
|
E:ALA390
|
4.2
|
48.5
|
1.0
|
CA
|
E:CYS391
|
4.3
|
48.5
|
1.0
|
N
|
E:CYS391
|
4.3
|
48.4
|
1.0
|
CZ
|
E:TYR355
|
4.4
|
48.5
|
1.0
|
N
|
E:MET357
|
4.4
|
47.9
|
1.0
|
O
|
E:GLY387
|
4.4
|
48.4
|
1.0
|
CE2
|
E:TYR355
|
4.5
|
48.3
|
1.0
|
CE
|
E:MET356
|
4.5
|
49.4
|
1.0
|
N
|
E:GLY359
|
4.5
|
48.2
|
1.0
|
CA
|
E:ALA390
|
4.6
|
48.4
|
1.0
|
CB
|
E:CYS391
|
4.6
|
48.4
|
1.0
|
C
|
E:ILE389
|
4.6
|
48.7
|
1.0
|
CG
|
E:GLU388
|
4.6
|
48.8
|
1.0
|
N
|
E:ILE389
|
4.7
|
48.7
|
1.0
|
CA
|
E:GLY359
|
4.8
|
48.2
|
1.0
|
CG
|
E:MET356
|
5.0
|
48.4
|
1.0
|
CB
|
E:GLU388
|
5.0
|
48.6
|
1.0
|
|
Sodium binding site 3 out
of 3 in 2wdr
Go back to
Sodium Binding Sites List in 2wdr
Sodium binding site 3 out
of 3 in the E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of E. Coli Succinate:Quinone Oxidoreductase (Sqr) with Pentachlorophenol Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Na1590
b:21.6
occ:1.00
|
O
|
I:GLU388
|
2.5
|
48.6
|
1.0
|
O
|
I:MET356
|
2.6
|
47.8
|
1.0
|
O
|
I:GLY358
|
2.7
|
48.4
|
1.0
|
O
|
I:ALA390
|
2.7
|
48.7
|
1.0
|
O
|
I:MET357
|
3.2
|
48.1
|
1.0
|
OH
|
I:TYR355
|
3.4
|
48.6
|
1.0
|
C
|
I:GLU388
|
3.5
|
48.6
|
1.0
|
C
|
I:MET357
|
3.5
|
48.0
|
1.0
|
C
|
I:MET356
|
3.8
|
47.9
|
1.0
|
C
|
I:ALA390
|
3.8
|
48.5
|
1.0
|
CA
|
I:GLU388
|
3.8
|
48.6
|
1.0
|
C
|
I:GLY358
|
3.8
|
48.3
|
1.0
|
CA
|
I:MET357
|
4.0
|
47.9
|
1.0
|
CZ
|
I:TYR355
|
4.0
|
48.6
|
1.0
|
N
|
I:GLY358
|
4.1
|
48.2
|
1.0
|
CE2
|
I:TYR355
|
4.2
|
48.3
|
1.0
|
CG
|
I:GLU388
|
4.3
|
48.8
|
1.0
|
N
|
I:MET357
|
4.4
|
47.9
|
1.0
|
O
|
I:GLY387
|
4.4
|
48.5
|
1.0
|
N
|
I:ALA390
|
4.4
|
48.6
|
1.0
|
CA
|
I:GLY358
|
4.5
|
48.3
|
1.0
|
CE
|
I:MET356
|
4.6
|
49.3
|
1.0
|
N
|
I:ILE389
|
4.6
|
48.6
|
1.0
|
N
|
I:CYS391
|
4.6
|
48.5
|
1.0
|
CA
|
I:CYS391
|
4.6
|
48.6
|
1.0
|
CB
|
I:GLU388
|
4.7
|
48.6
|
1.0
|
C
|
I:ILE389
|
4.7
|
48.7
|
1.0
|
CA
|
I:ALA390
|
4.7
|
48.6
|
1.0
|
N
|
I:GLY359
|
4.9
|
48.3
|
1.0
|
CG
|
I:MET356
|
5.0
|
48.4
|
1.0
|
N
|
I:GLU388
|
5.0
|
48.6
|
1.0
|
|
Reference:
J.Ruprecht,
V.Yankovskaya,
E.Maklashina,
S.Iwata,
G.Cecchini.
Structure of Escherichia Coli Succinate:Quinone Oxidoreductase with An Occupied and Empty Quinone- Binding Site. J.Biol.Chem. V. 284 29836 2009.
ISSN: ISSN 0021-9258
PubMed: 19710024
DOI: 10.1074/JBC.M109.010058
Page generated: Mon Oct 7 04:37:32 2024
|