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Magnesium in PDB 1z5g: Crystal Structure of Salmonella Typhimurium Apha Protein

Enzymatic activity of Crystal Structure of Salmonella Typhimurium Apha Protein

All present enzymatic activity of Crystal Structure of Salmonella Typhimurium Apha Protein:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Salmonella Typhimurium Apha Protein, PDB code: 1z5g was solved by R.D.Makde, V.Kumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.840, 84.590, 149.420, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 19.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Salmonella Typhimurium Apha Protein (pdb code 1z5g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Salmonella Typhimurium Apha Protein, PDB code: 1z5g:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1z5g

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Magnesium binding site 1 out of 4 in the Crystal Structure of Salmonella Typhimurium Apha Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Salmonella Typhimurium Apha Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:20.2
occ:1.00
O A:HOH644 1.9 17.0 1.0
OD2 A:ASP46 2.0 21.7 1.0
OD1 A:ASP169 2.1 17.8 1.0
O A:HOH647 2.1 17.3 1.0
O A:HOH643 2.1 16.6 1.0
O A:ASP48 2.2 15.3 1.0
CG A:ASP46 3.0 21.6 1.0
CG A:ASP169 3.1 17.0 1.0
OD1 A:ASP46 3.3 18.1 1.0
C A:ASP48 3.3 14.5 1.0
OD2 A:ASP169 3.5 17.7 1.0
OG A:SER170 3.9 17.1 1.0
OG1 A:THR50 4.0 18.2 1.0
OD2 A:ASP173 4.0 17.3 1.0
CA A:ASP48 4.1 14.8 1.0
O A:HOH710 4.1 34.7 1.0
N A:ASP48 4.2 15.4 1.0
CB A:ASP46 4.3 19.9 1.0
CB A:ASP48 4.3 17.4 1.0
O A:HOH642 4.3 22.2 1.0
O A:HOH648 4.4 32.7 1.0
N A:ASP49 4.4 16.1 1.0
CB A:ASP169 4.5 12.2 1.0
CB A:ASP49 4.5 15.6 1.0
N A:ASP169 4.6 15.7 1.0
N A:SER170 4.7 15.6 1.0
N A:THR50 4.7 18.0 1.0
CA A:ASP49 4.8 18.0 1.0
CB A:SER170 4.8 17.1 1.0
C A:ASP49 4.9 18.4 1.0
C A:ILE47 4.9 15.3 1.0
O A:HOH645 4.9 20.1 1.0
CB A:THR50 4.9 18.1 1.0
O A:HOH646 5.0 28.4 1.0
CA A:ASP169 5.0 14.0 1.0

Magnesium binding site 2 out of 4 in 1z5g

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Magnesium binding site 2 out of 4 in the Crystal Structure of Salmonella Typhimurium Apha Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Salmonella Typhimurium Apha Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:21.1
occ:1.00
O B:HOH641 2.0 19.1 1.0
O B:ASP48 2.1 14.8 1.0
OD1 B:ASP169 2.1 19.2 1.0
OD2 B:ASP46 2.1 18.6 1.0
O B:HOH645 2.1 18.6 1.0
O B:HOH644 2.3 21.9 1.0
CG B:ASP169 3.1 17.7 1.0
CG B:ASP46 3.1 18.3 1.0
C B:ASP48 3.2 17.4 1.0
OD2 B:ASP169 3.4 16.9 1.0
OD1 B:ASP46 3.4 19.9 1.0
OG1 B:THR50 3.9 16.6 1.0
OG B:SER170 4.0 23.2 1.0
CA B:ASP48 4.0 17.1 1.0
O B:HOH688 4.0 45.8 1.0
N B:ASP48 4.1 16.6 1.0
CB B:ASP48 4.2 17.8 1.0
OD2 B:ASP173 4.2 21.5 1.0
O B:HOH639 4.2 17.7 1.0
N B:ASP49 4.3 17.2 1.0
CB B:ASP49 4.4 17.1 1.0
CB B:ASP46 4.4 19.9 1.0
CB B:ASP169 4.4 19.0 1.0
O B:HOH646 4.4 38.0 1.0
N B:ASP169 4.6 17.6 1.0
CA B:ASP49 4.7 18.9 1.0
N B:THR50 4.7 17.2 1.0
C B:ASP49 4.7 19.1 1.0
N B:SER170 4.8 19.2 1.0
C B:ILE47 4.8 16.6 1.0
O B:HOH642 4.8 24.4 1.0
CB B:THR50 4.9 15.4 1.0
CB B:SER170 4.9 20.1 1.0
O B:HOH643 4.9 28.9 1.0
CA B:ASP169 5.0 18.2 1.0

Magnesium binding site 3 out of 4 in 1z5g

Go back to Magnesium Binding Sites List in 1z5g
Magnesium binding site 3 out of 4 in the Crystal Structure of Salmonella Typhimurium Apha Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Salmonella Typhimurium Apha Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg603

b:20.3
occ:1.00
OD2 C:ASP46 1.9 23.5 1.0
O C:HOH653 2.0 16.9 1.0
O C:ASP48 2.1 14.0 1.0
O C:HOH652 2.1 21.1 1.0
OD1 C:ASP169 2.1 18.9 1.0
O C:HOH650 2.3 22.3 1.0
CG C:ASP46 2.9 25.8 1.0
CG C:ASP169 3.1 17.4 1.0
C C:ASP48 3.2 16.0 1.0
OD1 C:ASP46 3.3 25.1 1.0
OD2 C:ASP169 3.4 15.7 1.0
OG1 C:THR50 3.9 14.5 1.0
CA C:ASP48 4.0 17.7 1.0
OG C:SER170 4.0 22.5 1.0
N C:ASP48 4.1 18.2 1.0
OD2 C:ASP173 4.1 20.7 1.0
O C:HOH692 4.2 53.4 1.0
CB C:ASP48 4.2 19.6 1.0
CB C:ASP46 4.2 23.0 1.0
O C:HOH648 4.2 23.0 1.0
N C:ASP49 4.3 16.6 1.0
O C:HOH651 4.4 33.3 1.0
CB C:ASP49 4.5 16.7 1.0
CB C:ASP169 4.5 15.7 1.0
N C:ASP169 4.6 17.8 1.0
N C:THR50 4.7 17.4 1.0
O C:HOH649 4.7 21.1 1.0
CA C:ASP49 4.7 18.4 1.0
C C:ASP49 4.8 18.0 1.0
O C:HOH654 4.8 34.2 1.0
C C:ILE47 4.8 19.4 1.0
CB C:THR50 4.8 16.4 1.0
N C:SER170 4.9 17.6 1.0
CB C:SER170 4.9 20.4 1.0
N C:ILE47 5.0 20.6 1.0

Magnesium binding site 4 out of 4 in 1z5g

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Magnesium binding site 4 out of 4 in the Crystal Structure of Salmonella Typhimurium Apha Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Salmonella Typhimurium Apha Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg604

b:18.9
occ:1.00
O D:ASP48 2.1 14.6 1.0
OD2 D:ASP46 2.1 18.4 1.0
O D:HOH660 2.1 15.3 1.0
OD1 D:ASP169 2.1 18.6 1.0
O D:HOH661 2.2 19.0 1.0
O3 D:PO4605 2.3 34.8 1.0
CG D:ASP46 3.1 17.5 1.0
CG D:ASP169 3.2 15.5 1.0
C D:ASP48 3.2 16.5 1.0
OD1 D:ASP46 3.5 18.1 1.0
OD2 D:ASP169 3.5 16.3 1.0
P D:PO4605 3.7 45.2 1.0
OG D:SER170 3.9 20.6 1.0
CA D:ASP48 3.9 15.0 1.0
OG1 D:THR50 4.0 14.6 1.0
O D:HOH705 4.1 38.6 1.0
N D:ASP48 4.1 15.6 1.0
CB D:ASP48 4.1 17.6 1.0
OD2 D:ASP173 4.1 18.2 1.0
O2 D:PO4605 4.2 33.1 1.0
O D:HOH662 4.2 21.0 1.0
N D:ASP49 4.3 15.0 1.0
O4 D:PO4605 4.4 37.6 1.0
O D:HOH704 4.4 46.6 1.0
CB D:ASP46 4.4 18.3 1.0
CB D:ASP49 4.5 15.1 1.0
CB D:ASP169 4.5 15.0 1.0
O1 D:PO4605 4.7 41.0 1.0
N D:ASP169 4.7 14.8 1.0
N D:THR50 4.7 15.6 1.0
CA D:ASP49 4.7 18.1 1.0
C D:ILE47 4.8 14.1 1.0
N D:SER170 4.8 15.6 1.0
C D:ASP49 4.8 16.9 1.0
CB D:SER170 4.9 18.4 1.0
CB D:THR50 4.9 14.8 1.0

Reference:

R.D.Makde, G.D.Gupta, S.K.Mahajan, V.Kumar. Structural and Mutational Analyses Reveal the Functional Role of Active-Site Lys-154 and Asp-173 of Salmonella Typhimurium Apha Protein. Arch.Biochem.Biophys. V. 464 70 2007.
ISSN: ISSN 0003-9861
PubMed: 17570338
DOI: 10.1016/J.ABB.2007.03.043
Page generated: Tue Aug 13 20:03:20 2024

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