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Magnesium in PDB 4own: Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium

Enzymatic activity of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium

All present enzymatic activity of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium:
2.4.2.18;

Protein crystallography data

The structure of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium, PDB code: 4own was solved by A.Castell, T.V.M.Cookson, F.L.Short, J.S.Lott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.35 / 2.11
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.585, 92.313, 120.826, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 19.4

Other elements in 4own:

The structure of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium (pdb code 4own). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium, PDB code: 4own:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4own

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Magnesium binding site 1 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:36.6
occ:1.00
 O A:HOH693 2.0 47.1 1.0
O A:HOH694 2.0 31.4 1.0
O A:HOH695 2.1 37.5 1.0
OD1 A:ASP251 2.1 29.5 1.0
OE2 A:GLU252 2.2 26.9 1.0
O A:HOH650 2.3 24.6 1.0
CG A:ASP251 3.0 27.2 1.0
CD A:GLU252 3.2 26.6 1.0
OD2 A:ASP251 3.2 28.4 1.0
MG A:MG402 3.3 20.4 1.0
CG A:GLU252 3.5 26.9 1.0
O5 A:POP403 3.7 27.4 1.0
OG1 A:THR115 3.9 41.9 1.0
OD2 A:ASP111 3.9 49.4 1.0
O A:HOH687 4.1 23.0 1.0
O A:ASP251 4.2 25.4 1.0
OD1 A:ASP111 4.2 56.5 1.0
OE1 A:GLU252 4.4 25.9 1.0
CG A:ASP111 4.4 50.2 1.0
CB A:ASP251 4.4 26.6 1.0
C A:ASP251 4.5 25.5 1.0
P2 A:POP403 4.8 29.8 1.0
O6 A:POP403 4.8 32.4 1.0
CA A:ASP251 4.8 26.8 1.0
N A:ASP251 4.8 27.4 1.0
O2 A:POP403 4.9 28.0 1.0
CB A:GLU252 5.0 25.9 1.0

Magnesium binding site 2 out of 4 in 4own

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Magnesium binding site 2 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:20.4
occ:1.00
 O5 A:POP403 1.9 27.4 1.0
O2 A:POP403 1.9 28.0 1.0
O A:HOH650 2.1 24.6 1.0
OG A:SER119 2.1 23.7 1.0
O A:HOH687 2.1 23.0 1.0
OE2 A:GLU252 2.2 26.9 1.0
CB A:SER119 3.0 22.9 1.0
P1 A:POP403 3.0 29.3 1.0
CD A:GLU252 3.2 26.6 1.0
P2 A:POP403 3.2 29.8 1.0
O A:POP403 3.3 29.0 1.0
MG A:MG401 3.3 36.6 1.0
OE1 A:GLU252 3.4 25.9 1.0
O A:HOH695 3.5 37.5 1.0
O3 A:POP403 3.7 31.8 1.0
N A:GLY107 4.0 24.9 1.0
OD2 A:ASP251 4.0 28.4 1.0
N A:SER119 4.0 23.0 1.0
CA A:SER119 4.1 22.8 1.0
O6 A:POP403 4.1 32.4 1.0
O4 A:POP403 4.3 28.6 1.0
CA A:GLY107 4.3 25.5 1.0
OD1 A:ASP251 4.3 29.5 1.0
O A:ASP251 4.3 25.4 1.0
O A:HOH557 4.3 27.7 1.0
O1 A:POP403 4.4 32.9 1.0
CG A:ASP251 4.4 27.2 1.0
CG A:GLU252 4.5 26.9 1.0
C A:VAL106 4.6 23.3 1.0
O A:HOH693 4.7 47.1 1.0
CA A:VAL106 4.9 21.8 1.0

Magnesium binding site 3 out of 4 in 4own

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Magnesium binding site 3 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:21.9
occ:1.00
 O1A B:PRP403 1.9 30.7 0.8
O B:HOH598 2.0 22.7 1.0
O3B B:PRP403 2.0 23.2 0.8
OG B:SER119 2.1 24.2 1.0
OE2 B:GLU252 2.2 32.3 1.0
O B:HOH606 2.2 19.6 1.0
CB B:SER119 3.0 22.9 1.0
CD B:GLU252 3.1 32.7 1.0
PA B:PRP403 3.1 29.7 0.8
PB B:PRP403 3.3 25.7 0.8
OE1 B:GLU252 3.3 33.2 1.0
MG B:MG402 3.4 43.3 1.0
O3A B:PRP403 3.5 29.0 0.8
O B:HOH647 3.7 47.9 1.0
N B:SER119 4.0 22.4 1.0
N B:GLY107 4.0 25.9 1.0
OD2 B:ASP251 4.0 28.0 1.0
O4 B:PRP403 4.1 48.9 0.8
CA B:SER119 4.1 21.7 1.0
O1 B:PRP403 4.1 35.8 0.8
O B:HOH559 4.2 28.4 1.0
OD1 B:ASP251 4.3 27.9 1.0
O2B B:PRP403 4.3 23.9 0.8
O1B B:PRP403 4.3 27.1 0.8
O B:ASP251 4.3 28.8 1.0
O2A B:PRP403 4.3 33.5 0.8
CG B:ASP251 4.4 28.5 1.0
C1 B:PRP403 4.4 43.1 0.8
CG B:GLU252 4.4 31.8 1.0
CA B:GLY107 4.4 26.9 1.0
C B:VAL106 4.7 25.5 1.0
CA B:VAL106 5.0 24.8 1.0

Magnesium binding site 4 out of 4 in 4own

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Magnesium binding site 4 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Fluoroanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:43.3
occ:1.00
 O B:HOH644 2.0 39.7 1.0
OD1 B:ASP251 2.2 27.9 1.0
OE2 B:GLU252 2.3 32.3 1.0
O B:HOH647 2.4 47.9 1.0
O B:HOH598 2.5 22.7 1.0
CG B:ASP251 3.2 28.5 1.0
CD B:GLU252 3.3 32.7 1.0
MG B:MG401 3.4 21.9 1.0
CG B:GLU252 3.5 31.8 1.0
OD2 B:ASP251 3.6 28.0 1.0
OD2 B:ASP111 3.6 45.8 1.0
O3B B:PRP403 3.9 23.2 0.8
OG1 B:THR115 4.1 39.8 1.0
O B:HOH636 4.1 47.8 1.0
O B:HOH606 4.3 19.6 1.0
CG B:ASP111 4.3 49.4 1.0
O B:ASP251 4.4 28.8 1.0
OE1 B:GLU252 4.4 33.2 1.0
O4 B:PRP403 4.5 48.9 0.8
OD1 B:ASP111 4.5 54.0 1.0
CB B:ASP251 4.5 28.2 1.0
C B:ASP251 4.6 29.2 1.0
N B:ASP251 4.7 31.2 1.0
CA B:ASP251 4.8 29.2 1.0
O1A B:PRP403 4.9 30.7 0.8
PB B:PRP403 4.9 25.7 0.8
O1B B:PRP403 5.0 27.1 0.8
CB B:GLU252 5.0 31.3 1.0

Reference:

T.V.Cookson, A.Castell, E.M.Bulloch, G.L.Evans, F.L.Short, E.N.Baker, J.S.Lott, E.J.Parker. Alternative Substrates Reveal Catalytic Cycle and Key Binding Events in the Reaction Catalysed By Anthranilate Phosphoribosyltransferase From Mycobacterium Tuberculosis. Biochem.J. V. 461 87 2014.
ISSN: ESSN 1470-8728
PubMed: 24712732
DOI: 10.1042/BJ20140209
Page generated: Tue Aug 20 01:00:36 2024

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