Atomistry » Sodium » PDB 5ddq-5dy9 » 5dmy
Atomistry »
  Sodium »
    PDB 5ddq-5dy9 »
      5dmy »

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:

Nickel (Ni) 1 atom
Magnesium (Mg) 5 atoms

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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy