Sodium in PDB 5dmy: Beta-Galactosidase - Construct 33-930
Enzymatic activity of Beta-Galactosidase - Construct 33-930
All present enzymatic activity of Beta-Galactosidase - Construct 33-930:
3.2.1.23;
Protein crystallography data
The structure of Beta-Galactosidase - Construct 33-930, PDB code: 5dmy
was solved by
K.A.Watson,
A.Lazidou,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
54.93 /
1.95
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
153.040,
52.650,
153.329,
90.00,
91.64,
90.00
|
R / Rfree (%)
|
19.8 /
26.4
|
Other elements in 5dmy:
The structure of Beta-Galactosidase - Construct 33-930 also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Beta-Galactosidase - Construct 33-930
(pdb code 5dmy). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the
Beta-Galactosidase - Construct 33-930, PDB code: 5dmy:
Jump to Sodium binding site number:
1;
2;
3;
Sodium binding site 1 out
of 3 in 5dmy
Go back to
Sodium Binding Sites List in 5dmy
Sodium binding site 1 out
of 3 in the Beta-Galactosidase - Construct 33-930
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na903
b:10.2
occ:1.00
|
OD1
|
A:ASP562
|
2.5
|
6.3
|
1.0
|
OG1
|
A:THR634
|
2.7
|
6.3
|
1.0
|
O
|
A:HOH1856
|
2.8
|
6.4
|
1.0
|
OD1
|
A:ASN539
|
2.9
|
8.0
|
1.0
|
O
|
A:HOH1500
|
3.1
|
5.9
|
1.0
|
O
|
A:HOH1581
|
3.4
|
10.0
|
1.0
|
CG
|
A:ASP562
|
3.4
|
4.7
|
1.0
|
CG2
|
A:THR634
|
3.5
|
3.3
|
1.0
|
CB
|
A:THR634
|
3.5
|
6.9
|
1.0
|
CB
|
A:ALA537
|
3.7
|
1.9
|
1.0
|
CG
|
A:ASN539
|
3.7
|
6.1
|
1.0
|
CB
|
A:ASP562
|
3.8
|
3.0
|
1.0
|
CA
|
A:ASP562
|
3.9
|
8.7
|
1.0
|
ND2
|
A:ASN539
|
4.0
|
4.2
|
1.0
|
CB
|
A:ALA572
|
4.0
|
3.0
|
1.0
|
O
|
A:HOH1566
|
4.3
|
15.1
|
1.0
|
OD2
|
A:ASP562
|
4.5
|
6.2
|
1.0
|
N
|
A:ALA572
|
4.6
|
3.2
|
1.0
|
O
|
A:HOH1527
|
4.6
|
5.7
|
1.0
|
O
|
A:HOH1048
|
4.7
|
4.3
|
1.0
|
O
|
A:HOH1018
|
4.7
|
6.2
|
1.0
|
N
|
A:ASP562
|
4.7
|
3.9
|
1.0
|
CB
|
A:ASN539
|
4.9
|
3.2
|
1.0
|
O
|
A:TYR561
|
4.9
|
8.8
|
1.0
|
O
|
A:HOH1503
|
4.9
|
8.1
|
1.0
|
C
|
A:ASP562
|
4.9
|
5.3
|
1.0
|
CA
|
A:THR634
|
4.9
|
3.0
|
1.0
|
CA
|
A:ALA572
|
5.0
|
3.9
|
1.0
|
|
Sodium binding site 2 out
of 3 in 5dmy
Go back to
Sodium Binding Sites List in 5dmy
Sodium binding site 2 out
of 3 in the Beta-Galactosidase - Construct 33-930
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Na902
b:18.1
occ:1.00
|
O
|
C:HOH1296
|
2.4
|
11.8
|
1.0
|
O
|
C:ASN643
|
2.4
|
9.9
|
1.0
|
OD2
|
C:ASP675
|
2.5
|
17.7
|
1.0
|
O
|
C:HOH1517
|
2.6
|
18.5
|
1.0
|
O
|
C:VAL646
|
2.6
|
13.9
|
1.0
|
O
|
C:HOH1587
|
2.6
|
18.2
|
1.0
|
CG
|
C:ASP675
|
3.3
|
15.0
|
1.0
|
C
|
C:ASN643
|
3.6
|
15.1
|
1.0
|
CB
|
C:ASP675
|
3.7
|
10.2
|
1.0
|
C
|
C:VAL646
|
3.8
|
11.6
|
1.0
|
CA
|
C:ASP644
|
4.1
|
20.9
|
1.0
|
CA
|
C:HIS647
|
4.2
|
16.0
|
1.0
|
OD1
|
C:ASP675
|
4.3
|
14.1
|
1.0
|
N
|
C:ASP644
|
4.3
|
18.0
|
1.0
|
ND1
|
C:HIS647
|
4.3
|
18.8
|
1.0
|
O
|
C:HOH1524
|
4.3
|
28.7
|
1.0
|
C
|
C:ASP644
|
4.4
|
19.9
|
1.0
|
O
|
C:GLN639
|
4.4
|
11.4
|
1.0
|
N
|
C:HIS647
|
4.5
|
8.7
|
1.0
|
N
|
C:VAL646
|
4.6
|
17.1
|
1.0
|
O
|
C:SER640
|
4.8
|
6.9
|
1.0
|
CA
|
C:ASN643
|
4.8
|
14.1
|
1.0
|
O
|
C:ASP644
|
4.8
|
19.9
|
1.0
|
N
|
C:ASP645
|
4.8
|
18.8
|
1.0
|
CA
|
C:VAL646
|
4.9
|
10.1
|
1.0
|
C
|
C:HIS647
|
5.0
|
11.1
|
1.0
|
|
Sodium binding site 3 out
of 3 in 5dmy
Go back to
Sodium Binding Sites List in 5dmy
Sodium binding site 3 out
of 3 in the Beta-Galactosidase - Construct 33-930
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Na903
b:15.9
occ:1.00
|
O
|
C:ASP595
|
2.5
|
8.0
|
1.0
|
O
|
C:HOH1393
|
2.6
|
15.6
|
1.0
|
OD1
|
C:ASP329
|
2.8
|
13.7
|
1.0
|
O
|
C:HOH1475
|
2.9
|
9.3
|
1.0
|
O
|
C:ASP329
|
3.5
|
10.9
|
1.0
|
C
|
C:ASP595
|
3.7
|
10.0
|
1.0
|
N
|
C:GLY331
|
3.8
|
16.1
|
1.0
|
CG
|
C:ASP329
|
3.9
|
16.3
|
1.0
|
CA
|
C:TYR596
|
3.9
|
7.3
|
1.0
|
NE2
|
C:GLN345
|
4.0
|
8.8
|
1.0
|
C
|
C:ASP329
|
4.2
|
14.6
|
1.0
|
CB
|
C:PHE594
|
4.2
|
9.4
|
1.0
|
N
|
C:TYR596
|
4.3
|
6.6
|
1.0
|
CA
|
C:GLY331
|
4.3
|
14.9
|
1.0
|
CG2
|
C:THR627
|
4.3
|
12.9
|
1.0
|
OD2
|
C:ASP329
|
4.4
|
17.8
|
1.0
|
CB
|
C:TYR596
|
4.4
|
5.4
|
1.0
|
CA
|
C:THR627
|
4.5
|
9.4
|
1.0
|
O
|
C:HOH1293
|
4.5
|
10.5
|
1.0
|
CD2
|
C:PHE594
|
4.6
|
10.5
|
1.0
|
C
|
C:GLN330
|
4.6
|
12.1
|
1.0
|
CA
|
C:GLN330
|
4.7
|
12.8
|
1.0
|
N
|
C:GLN330
|
4.7
|
14.7
|
1.0
|
CB
|
C:THR627
|
4.7
|
16.9
|
1.0
|
O
|
C:THR627
|
4.8
|
10.8
|
1.0
|
C
|
C:PHE594
|
4.8
|
8.9
|
1.0
|
CA
|
C:ASP595
|
4.9
|
10.8
|
1.0
|
N
|
C:ASP595
|
4.9
|
8.4
|
1.0
|
CG
|
C:PHE594
|
4.9
|
14.5
|
1.0
|
O
|
C:PHE594
|
5.0
|
8.9
|
1.0
|
C
|
C:TYR596
|
5.0
|
10.8
|
1.0
|
CB
|
C:ASP329
|
5.0
|
11.7
|
1.0
|
|
Reference:
A.Lazidou,
D.Charalampopoulos,
K.A.Watson.
Rational Protein Engineering Toward the Development of A Beta-Galactosidase with Improved Functional Properties To Be Published.
Page generated: Mon Oct 7 20:38:41 2024
|