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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

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