Atomistry » Magnesium » PDB 5dji-5ds5 » 5dmy
Atomistry »
  Magnesium »
    PDB 5dji-5ds5 »
      5dmy »

Magnesium 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
Sodium (Na) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Beta-Galactosidase - Construct 33-930 (pdb code 5dmy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Beta-Galactosidase - Construct 33-930, PDB code: 5dmy:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 5dmy

Go back to Magnesium Binding Sites List in 5dmy
Magnesium binding site 1 out of 5 in the Beta-Galactosidase - Construct 33-930


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:8.2
occ:1.00
O A:VAL646 2.2 9.9 1.0
O A:ASN643 2.3 4.2 1.0
O A:HOH1331 2.4 5.6 1.0
O A:HOH1703 2.5 12.9 1.0
O A:HOH1682 2.5 17.8 1.0
OD2 A:ASP675 2.6 6.9 1.0
CG A:ASP675 3.4 6.4 1.0
C A:VAL646 3.4 6.5 1.0
C A:ASN643 3.5 6.5 1.0
CB A:ASP675 3.9 7.4 1.0
CA A:ASP644 4.0 9.9 1.0
CA A:HIS647 4.0 6.6 1.0
O A:HOH1309 4.0 16.9 1.0
N A:HIS647 4.2 6.5 1.0
N A:ASP644 4.2 9.5 1.0
OD1 A:ASP675 4.2 5.3 1.0
ND1 A:HIS647 4.2 8.3 1.0
N A:VAL646 4.3 9.8 1.0
O A:GLN639 4.4 2.9 1.0
C A:ASP644 4.4 10.8 1.0
CA A:VAL646 4.5 8.1 1.0
CA A:ASN643 4.6 5.3 1.0
CG2 A:VAL646 4.7 7.1 1.0
OD1 A:ASP644 4.7 24.5 1.0
N A:ASP645 4.7 8.3 1.0
C A:HIS647 4.8 5.2 1.0
CB A:ASN643 4.9 5.2 1.0
N A:ASN643 4.9 3.6 1.0
N A:THR648 4.9 6.1 1.0
OG1 A:THR648 4.9 4.5 1.0
CE1 A:HIS647 5.0 9.7 1.0
CG A:HIS647 5.0 9.8 1.0
O A:ASP644 5.0 9.7 1.0

Magnesium binding site 2 out of 5 in 5dmy

Go back to Magnesium Binding Sites List in 5dmy
Magnesium binding site 2 out of 5 in the Beta-Galactosidase - Construct 33-930


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:10.2
occ:1.00
OE1 A:GLN330 2.6 3.4 1.0
O A:HOH1396 2.7 3.8 1.0
O A:HOH1184 2.7 3.7 1.0
O A:HOH1269 3.0 3.2 1.0
NE2 A:GLN345 3.4 2.4 1.0
CA A:GLN330 3.5 4.0 1.0
CD A:GLN330 3.5 4.1 1.0
CB A:GLN330 3.6 2.6 1.0
CG A:GLN345 3.7 2.0 1.0
O A:HOH1327 3.7 4.9 1.0
CD A:GLN345 3.7 2.0 1.0
C A:GLN330 3.8 3.3 1.0
O A:GLN330 3.9 3.6 1.0
O A:ALA341 4.0 2.9 1.0
CG A:GLN330 4.2 8.5 1.0
CB A:ALA341 4.4 1.8 1.0
OH A:TYR789 4.4 3.1 1.0
C A:ALA341 4.5 2.5 1.0
NE2 A:GLN330 4.5 6.8 1.0
N A:GLY331 4.5 3.1 1.0
OE1 A:GLN345 4.6 1.4 1.0
O A:THR627 4.7 3.8 1.0
NH1 A:ARG344 4.7 2.7 1.0
CA A:ALA341 4.7 2.4 1.0
CE2 A:PHE594 4.8 4.8 1.0
N A:GLN330 4.9 4.6 1.0
O A:ASP329 4.9 4.3 1.0
CD2 A:PHE594 5.0 4.4 1.0

Magnesium binding site 3 out of 5 in 5dmy

Go back to Magnesium Binding Sites List in 5dmy
Magnesium binding site 3 out of 5 in the Beta-Galactosidase - Construct 33-930


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg901

b:9.5
occ:1.00
OD1 B:ASN394 2.1 15.9 1.0
O B:THR606 2.3 16.7 1.0
O B:HOH1167 2.4 18.7 1.0
O B:ASN392 2.5 15.1 1.0
OE1 B:GLU79 2.6 16.5 1.0
OE1 B:GLU81 2.7 17.7 1.0
CG B:ASN394 3.2 13.2 1.0
C B:THR606 3.4 18.5 1.0
CD B:GLU79 3.4 17.0 1.0
OE2 B:GLU79 3.6 16.2 1.0
C B:ASN392 3.6 16.7 1.0
ND2 B:ASN394 3.8 8.4 1.0
CD B:GLU81 3.9 14.4 1.0
C B:GLY393 4.1 15.9 1.0
CA B:THR606 4.1 19.4 1.0
O B:HOH1508 4.1 18.2 1.0
O B:HOH1165 4.2 15.0 1.0
N B:ASN394 4.2 10.2 1.0
CB B:ASN392 4.2 12.0 1.0
O B:GLY393 4.3 20.9 1.0
CB B:PRO162 4.4 12.0 1.0
CB B:THR606 4.4 18.2 1.0
CB B:ASN394 4.4 13.2 1.0
N B:GLY393 4.5 13.3 1.0
CA B:GLY393 4.5 11.5 1.0
N B:GLY607 4.5 19.5 1.0
CA B:ASN394 4.5 13.8 1.0
CA B:ASN392 4.6 18.0 1.0
OE2 B:GLU81 4.7 12.6 1.0
CA B:GLY607 4.7 19.2 1.0
CG B:GLU81 4.8 21.2 1.0
CG B:GLU79 4.8 15.1 1.0

Magnesium binding site 4 out of 5 in 5dmy

Go back to Magnesium Binding Sites List in 5dmy
Magnesium binding site 4 out of 5 in the Beta-Galactosidase - Construct 33-930


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg902

b:12.8
occ:1.00
O B:VAL646 2.3 15.5 1.0
O B:HOH1346 2.3 7.1 1.0
O B:HOH1457 2.4 9.9 1.0
O B:ASN643 2.4 12.7 1.0
OD2 B:ASP675 2.5 9.3 1.0
O B:HOH1244 3.1 25.1 1.0
CG B:ASP675 3.2 12.3 1.0
C B:VAL646 3.4 11.0 1.0
C B:ASN643 3.6 13.3 1.0
CB B:ASP675 3.8 12.8 1.0
CA B:HIS647 4.0 11.3 1.0
OD1 B:ASP675 4.0 12.7 1.0
CA B:ASP644 4.1 13.2 1.0
N B:HIS647 4.2 13.6 1.0
ND1 B:HIS647 4.3 15.1 1.0
N B:ASP644 4.3 11.8 1.0
N B:VAL646 4.4 15.6 1.0
OD1 B:ASP644 4.5 32.2 1.0
O B:GLN639 4.5 9.1 1.0
C B:ASP644 4.5 16.2 1.0
CA B:VAL646 4.5 14.4 1.0
C B:HIS647 4.7 12.2 1.0
CG2 B:VAL646 4.7 11.9 1.0
N B:THR648 4.8 9.2 1.0
CA B:ASN643 4.8 12.2 1.0
N B:ASP645 4.8 13.1 1.0
O B:SER640 5.0 11.8 1.0
CG B:HIS647 5.0 17.0 1.0
CB B:HIS647 5.0 17.9 1.0

Magnesium binding site 5 out of 5 in 5dmy

Go back to Magnesium Binding Sites List in 5dmy
Magnesium binding site 5 out of 5 in the Beta-Galactosidase - Construct 33-930


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Beta-Galactosidase - Construct 33-930 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg901

b:9.5
occ:1.00
O C:HOH1001 1.7 16.8 1.0
O C:THR606 2.2 11.0 1.0
O C:ASN392 2.3 16.4 1.0
OD1 C:ASN394 2.4 10.8 1.0
OE1 C:GLU81 2.4 7.2 1.0
O C:HOH1254 2.5 10.9 1.0
OE1 C:GLU79 2.7 18.0 1.0
C C:THR606 3.3 18.5 1.0
CD C:GLU81 3.5 17.4 1.0
CG C:ASN394 3.5 10.6 1.0
C C:ASN392 3.6 14.9 1.0
CD C:GLU79 3.6 22.0 1.0
OE2 C:GLU79 3.7 16.3 1.0
O C:HOH1408 3.8 20.0 1.0
CA C:THR606 3.9 16.6 1.0
CB C:ASN392 4.0 13.1 1.0
ND2 C:ASN394 4.1 12.1 1.0
CB C:THR606 4.2 25.6 1.0
O C:HOH1161 4.2 22.2 1.0
C C:GLY393 4.2 12.0 1.0
OE2 C:GLU81 4.2 18.6 1.0
N C:ASN394 4.3 11.2 1.0
N C:GLY607 4.4 15.5 1.0
CA C:ASN392 4.4 11.5 1.0
O C:GLY393 4.4 13.6 1.0
CG C:GLU81 4.5 24.0 1.0
CB C:PRO162 4.5 13.9 1.0
N C:GLY393 4.5 11.3 1.0
CA C:GLY393 4.5 10.7 1.0
CA C:ASN394 4.7 11.7 1.0
CB C:ASN394 4.7 11.4 1.0
CA C:GLY607 4.7 16.9 1.0
CB C:GLU81 4.9 16.6 1.0
CG C:PRO162 4.9 15.3 1.0
CG C:GLU79 4.9 13.0 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: Sun Sep 29 02:52:25 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