Sodium in PDB 3hwx: Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Enzymatic activity of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
All present enzymatic activity of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp:
2.2.1.9;
Protein crystallography data
The structure of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp, PDB code: 3hwx
was solved by
A.Priyadarshi,
K.Y.Hwang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.69 /
2.60
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
90.353,
90.463,
169.170,
75.99,
83.00,
64.15
|
R / Rfree (%)
|
19.7 /
25.3
|
Other elements in 3hwx:
The structure of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp also contains other interesting chemical elements:
Sodium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
15;
Binding sites:
The binding sites of Sodium atom in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
(pdb code 3hwx). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 15 binding sites of Sodium where determined in the
Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp, PDB code: 3hwx:
Jump to Sodium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Sodium binding site 1 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 1 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na557
b:17.3
occ:1.00
|
CG
|
A:GLN71
|
3.6
|
11.1
|
1.0
|
CA
|
A:GLN71
|
3.8
|
8.9
|
1.0
|
CB
|
A:GLN71
|
3.9
|
8.7
|
1.0
|
CD
|
A:PRO72
|
3.9
|
6.7
|
1.0
|
O
|
A:GLY22
|
4.1
|
5.8
|
1.0
|
O
|
A:LYS70
|
4.2
|
9.0
|
1.0
|
CA
|
A:GLY22
|
4.2
|
4.3
|
1.0
|
C
|
A:GLY22
|
4.6
|
4.9
|
1.0
|
N
|
A:GLN71
|
4.6
|
9.1
|
1.0
|
N
|
A:PRO72
|
4.7
|
6.9
|
1.0
|
O
|
A:HIS21
|
4.7
|
2.5
|
1.0
|
C
|
A:GLN71
|
4.8
|
7.7
|
1.0
|
C
|
A:LYS70
|
4.8
|
9.1
|
1.0
|
CG
|
A:PRO72
|
4.9
|
6.3
|
1.0
|
CD
|
A:GLN71
|
4.9
|
14.2
|
1.0
|
|
Sodium binding site 2 out
of 15 in 3hwx
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Sodium Binding Sites List in 3hwx
Sodium binding site 2 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na558
b:23.9
occ:1.00
|
N
|
A:ALA203
|
3.7
|
12.4
|
1.0
|
O
|
A:ARG201
|
3.8
|
13.1
|
1.0
|
C
|
A:ARG201
|
3.9
|
13.2
|
1.0
|
CB
|
A:ALA203
|
4.1
|
13.3
|
1.0
|
N
|
A:GLU202
|
4.1
|
12.2
|
1.0
|
CB
|
A:ARG201
|
4.1
|
14.1
|
1.0
|
CD2
|
I:LEU326
|
4.1
|
9.2
|
1.0
|
CA
|
A:GLU202
|
4.3
|
11.6
|
1.0
|
C
|
A:GLU202
|
4.3
|
11.9
|
1.0
|
CA
|
A:ALA203
|
4.3
|
13.2
|
1.0
|
NE2
|
I:GLN211
|
4.4
|
15.4
|
1.0
|
O
|
A:ALA203
|
4.5
|
14.1
|
1.0
|
C
|
A:ALA203
|
4.5
|
13.8
|
1.0
|
CA
|
A:ARG201
|
4.6
|
13.5
|
1.0
|
OE1
|
I:GLN211
|
4.6
|
18.9
|
1.0
|
O
|
I:ARG325
|
4.8
|
7.2
|
1.0
|
CD
|
I:GLN211
|
4.9
|
17.1
|
1.0
|
OG
|
I:SER208
|
5.0
|
19.7
|
1.0
|
|
Sodium binding site 3 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 3 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na557
b:30.6
occ:1.00
|
N
|
B:ARG510
|
3.5
|
12.6
|
1.0
|
CA
|
B:HIS509
|
3.7
|
11.1
|
1.0
|
C
|
B:HIS509
|
4.1
|
12.0
|
1.0
|
O
|
B:TYR508
|
4.1
|
10.1
|
1.0
|
CB
|
B:HIS509
|
4.2
|
11.1
|
1.0
|
ND1
|
B:HIS509
|
4.2
|
11.7
|
1.0
|
CA
|
B:ARG510
|
4.5
|
13.5
|
1.0
|
N
|
B:HIS509
|
4.6
|
10.6
|
1.0
|
CG
|
B:HIS509
|
4.7
|
11.9
|
1.0
|
C
|
B:TYR508
|
4.7
|
10.8
|
1.0
|
C
|
B:ARG510
|
4.8
|
13.5
|
1.0
|
O
|
B:ARG510
|
4.9
|
13.4
|
1.0
|
CB
|
B:ARG510
|
4.9
|
13.6
|
1.0
|
CD2
|
B:TYR508
|
4.9
|
7.9
|
1.0
|
|
Sodium binding site 4 out
of 15 in 3hwx
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Sodium Binding Sites List in 3hwx
Sodium binding site 4 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 4 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Na557
b:20.4
occ:1.00
|
N
|
I:HIS49
|
3.4
|
15.1
|
1.0
|
O
|
I:HIS49
|
3.9
|
13.1
|
1.0
|
NH1
|
J:ARG487
|
4.0
|
18.7
|
1.0
|
ND1
|
I:HIS49
|
4.0
|
18.5
|
1.0
|
CA
|
I:ILE48
|
4.1
|
14.7
|
1.0
|
NH2
|
J:ARG487
|
4.2
|
21.8
|
1.0
|
C
|
I:ILE48
|
4.2
|
15.7
|
1.0
|
CA
|
I:HIS49
|
4.3
|
13.9
|
1.0
|
CG2
|
I:ILE48
|
4.3
|
12.4
|
1.0
|
CB
|
I:HIS49
|
4.4
|
14.7
|
1.0
|
O
|
I:PHE47
|
4.5
|
14.7
|
1.0
|
CZ
|
J:ARG487
|
4.6
|
20.9
|
1.0
|
C
|
I:HIS49
|
4.6
|
13.2
|
1.0
|
CG
|
I:HIS49
|
4.6
|
16.9
|
1.0
|
CB
|
I:ILE48
|
4.7
|
14.4
|
1.0
|
|
Sodium binding site 5 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 5 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 5 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Na558
b:17.7
occ:1.00
|
O
|
I:ASP378
|
4.2
|
17.4
|
1.0
|
CA
|
I:ASP378
|
4.7
|
17.5
|
1.0
|
C
|
I:ASP378
|
4.9
|
17.2
|
1.0
|
|
Sodium binding site 6 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 6 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 6 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Na559
b:18.6
occ:1.00
|
N
|
I:GLU382
|
3.9
|
15.7
|
1.0
|
CB
|
I:TRP525
|
3.9
|
19.1
|
1.0
|
CG
|
I:TRP525
|
3.9
|
17.1
|
1.0
|
CD2
|
I:TRP525
|
4.2
|
13.7
|
1.0
|
O
|
I:GLU382
|
4.2
|
16.0
|
1.0
|
CB
|
I:GLU382
|
4.4
|
16.9
|
1.0
|
CB
|
I:PRO381
|
4.5
|
13.3
|
1.0
|
CD1
|
I:TRP525
|
4.5
|
16.4
|
1.0
|
CA
|
I:PRO381
|
4.5
|
13.8
|
1.0
|
CE3
|
I:TRP525
|
4.5
|
13.4
|
1.0
|
CA
|
I:GLU382
|
4.6
|
16.5
|
1.0
|
C
|
I:PRO381
|
4.6
|
15.0
|
1.0
|
CB
|
I:PRO435
|
4.8
|
12.6
|
1.0
|
CG
|
I:PRO435
|
4.8
|
11.1
|
1.0
|
CE2
|
I:TRP525
|
4.8
|
12.9
|
1.0
|
C
|
I:GLU382
|
4.9
|
15.8
|
1.0
|
O
|
I:TRP525
|
4.9
|
17.1
|
1.0
|
NE1
|
I:TRP525
|
5.0
|
15.5
|
1.0
|
|
Sodium binding site 7 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 7 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 7 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Na557
b:29.5
occ:1.00
|
NH2
|
R:ARG430
|
3.3
|
8.0
|
1.0
|
CG
|
R:GLN457
|
3.5
|
16.7
|
1.0
|
CD
|
R:GLN457
|
3.5
|
18.6
|
1.0
|
OE1
|
R:GLN457
|
3.8
|
15.8
|
1.0
|
CB
|
R:GLN457
|
3.8
|
13.5
|
1.0
|
CA
|
R:LEU454
|
4.0
|
8.2
|
1.0
|
NE2
|
R:GLN457
|
4.1
|
16.6
|
1.0
|
O
|
R:LEU454
|
4.1
|
8.3
|
1.0
|
CD2
|
R:LEU454
|
4.2
|
8.5
|
1.0
|
CZ
|
R:ARG430
|
4.3
|
8.3
|
1.0
|
O
|
R:ALA453
|
4.3
|
6.9
|
1.0
|
NH1
|
R:ARG430
|
4.4
|
9.0
|
1.0
|
C
|
R:LEU454
|
4.5
|
8.6
|
1.0
|
O
|
R:THR51
|
4.7
|
11.0
|
1.0
|
N
|
R:LEU454
|
4.7
|
7.6
|
1.0
|
CB
|
R:LEU454
|
4.8
|
7.9
|
1.0
|
C
|
R:ALA453
|
4.8
|
7.0
|
1.0
|
N
|
R:GLN457
|
4.9
|
13.7
|
1.0
|
CA
|
R:GLN457
|
4.9
|
13.5
|
1.0
|
CG
|
R:LEU454
|
5.0
|
8.8
|
1.0
|
|
Sodium binding site 8 out
of 15 in 3hwx
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Sodium Binding Sites List in 3hwx
Sodium binding site 8 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 8 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Na558
b:34.7
occ:1.00
|
O
|
R:GLY190
|
3.6
|
19.1
|
1.0
|
OE1
|
R:GLN194
|
4.2
|
25.0
|
1.0
|
C
|
R:GLY190
|
4.2
|
18.6
|
1.0
|
CG
|
R:GLN187
|
4.6
|
21.2
|
1.0
|
CD1
|
R:TRP193
|
4.7
|
19.3
|
1.0
|
CA
|
R:GLY190
|
4.8
|
18.7
|
1.0
|
NE2
|
R:GLN194
|
4.8
|
23.3
|
1.0
|
CA
|
R:GLN187
|
4.8
|
21.5
|
1.0
|
N
|
R:ASP191
|
4.9
|
18.0
|
1.0
|
O
|
R:GLN187
|
4.9
|
21.4
|
1.0
|
CB
|
R:TRP193
|
4.9
|
15.9
|
1.0
|
CD
|
R:GLN194
|
4.9
|
23.3
|
1.0
|
CB
|
R:GLN187
|
4.9
|
21.6
|
1.0
|
|
Sodium binding site 9 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 9 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 9 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Na559
b:26.7
occ:1.00
|
CE2
|
R:PHE216
|
3.3
|
15.7
|
1.0
|
CD2
|
R:PHE216
|
3.5
|
12.9
|
1.0
|
OD2
|
R:ASP213
|
3.7
|
23.0
|
1.0
|
NE1
|
R:TRP217
|
3.8
|
15.3
|
1.0
|
CZ
|
R:PHE216
|
4.0
|
16.7
|
1.0
|
CZ2
|
R:TRP217
|
4.2
|
13.7
|
1.0
|
CG
|
R:PHE216
|
4.2
|
14.6
|
1.0
|
CE2
|
R:TRP217
|
4.2
|
15.0
|
1.0
|
CG
|
R:ASP213
|
4.5
|
21.9
|
1.0
|
CB
|
R:ASP213
|
4.6
|
20.3
|
1.0
|
CE1
|
R:PHE216
|
4.6
|
17.0
|
1.0
|
CD1
|
R:PHE216
|
4.7
|
15.7
|
1.0
|
CD1
|
R:TRP217
|
4.7
|
13.3
|
1.0
|
|
Sodium binding site 10 out
of 15 in 3hwx
Go back to
Sodium Binding Sites List in 3hwx
Sodium binding site 10 out
of 15 in the Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 10 of Crystal Structure of Menaquinone Synthesis Protein Mend From E. Coli in Complex with Thdp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Na557
b:19.3
occ:1.00
|
CD2
|
S:HIS499
|
3.1
|
12.2
|
1.0
|
CB
|
S:HIS496
|
3.4
|
6.8
|
1.0
|
O
|
S:HIS496
|
3.6
|
5.7
|
1.0
|
C
|
S:HIS496
|
3.6
|
6.2
|
1.0
|
N
|
S:HIS499
|
3.7
|
9.2
|
1.0
|
CG
|
S:HIS499
|
3.8
|
11.3
|
1.0
|
CA
|
S:HIS496
|
3.9
|
6.5
|
1.0
|
CB
|
S:HIS499
|
4.0
|
8.2
|
1.0
|
N
|
S:GLU498
|
4.0
|
9.0
|
1.0
|
N
|
S:PHE497
|
4.1
|
6.2
|
1.0
|
N
|
S:HIS496
|
4.2
|
5.7
|
1.0
|
NE2
|
S:HIS499
|
4.3
|
12.2
|
1.0
|
CB
|
S:GLU498
|
4.3
|
10.3
|
1.0
|
CA
|
R:MET503
|
4.5
|
10.8
|
1.0
|
CA
|
S:HIS499
|
4.5
|
8.3
|
1.0
|
CA
|
S:GLU498
|
4.5
|
9.8
|
1.0
|
C
|
S:GLU498
|
4.6
|
9.6
|
1.0
|
CB
|
R:MET503
|
4.7
|
11.5
|
1.0
|
CG
|
S:HIS496
|
4.7
|
8.3
|
1.0
|
C
|
S:PHE497
|
4.7
|
8.0
|
1.0
|
CA
|
S:PHE497
|
4.8
|
7.4
|
1.0
|
NH2
|
S:ARG510
|
4.9
|
25.4
|
1.0
|
|
Reference:
A.Priyadarshi,
E.E.Kim,
K.Y.Hwang.
Structural and Functional Analysis of Vitamin K2 Synthesis Protein Mend. Biochem.Biophys.Res.Commun. V. 388 748 2009.
ISSN: ISSN 0006-291X
PubMed: 19703421
DOI: 10.1016/J.BBRC.2009.08.093
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