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

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

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

Protein crystallography data

The structure of Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, Prpp and Magnesium, PDB code: 4owu 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) 73.09 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.486, 91.792, 120.801, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, Prpp and Magnesium (pdb code 4owu). 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-Methylanthranilate, Prpp and Magnesium, PDB code: 4owu:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4owu

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Magnesium binding site 1 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, 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-Methylanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:30.1
occ:1.00
 OE2 A:GLU252 2.3 19.9 1.0
O A:HOH736 2.3 27.3 1.0
O A:HOH738 2.3 41.5 1.0
OD1 A:ASP251 2.4 21.6 1.0
O A:HOH670 2.5 18.8 1.0
CD A:GLU252 3.2 21.6 1.0
CG A:ASP251 3.3 20.5 1.0
CG A:GLU252 3.4 21.1 1.0
MG A:MG402 3.4 20.3 1.0
OD2 A:ASP251 3.5 21.0 1.0
O2B A:PRP403 3.6 21.5 1.0
OD2 A:ASP111 3.8 38.6 1.0
O A:HOH737 3.8 39.7 1.0
OG1 A:THR115 4.1 34.8 1.0
O A:HOH723 4.2 17.0 1.0
O A:HOH739 4.3 39.0 1.0
O A:ASP251 4.3 18.8 1.0
OE1 A:GLU252 4.4 20.8 1.0
C A:ASP251 4.6 20.6 1.0
CB A:ASP251 4.6 20.0 1.0
CG A:ASP111 4.7 36.5 1.0
O3B A:PRP403 4.8 25.9 1.0
PB A:PRP403 4.8 24.1 1.0
N A:ASP251 4.8 20.7 1.0
O4 A:PRP403 4.8 32.9 1.0
CB A:GLU252 4.9 21.0 1.0
CA A:ASP251 4.9 20.3 1.0
O2A A:PRP403 4.9 23.1 1.0

Magnesium binding site 2 out of 4 in 4owu

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Magnesium binding site 2 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, 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-Methylanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:20.3
occ:1.00
 O2A A:PRP403 2.0 23.1 1.0
O A:HOH723 2.0 17.0 1.0
O2B A:PRP403 2.0 21.5 1.0
OG A:SER119 2.1 18.1 1.0
OE2 A:GLU252 2.1 19.9 1.0
O A:HOH670 2.1 18.8 1.0
CB A:SER119 3.0 17.6 1.0
CD A:GLU252 3.0 21.6 1.0
PA A:PRP403 3.2 25.4 1.0
OE1 A:GLU252 3.3 20.8 1.0
PB A:PRP403 3.3 24.1 1.0
MG A:MG401 3.4 30.1 1.0
O3A A:PRP403 3.6 28.1 1.0
N A:GLY107 3.9 18.9 1.0
O A:HOH736 3.9 27.3 1.0
OD2 A:ASP251 4.0 21.0 1.0
N A:SER119 4.0 18.3 1.0
CA A:SER119 4.1 18.2 1.0
O A:ASP251 4.2 18.8 1.0
O1 A:PRP403 4.3 28.8 1.0
O A:HOH563 4.3 21.8 1.0
O3B A:PRP403 4.3 25.9 1.0
O1B A:PRP403 4.3 23.4 1.0
CA A:GLY107 4.4 18.6 1.0
CG A:GLU252 4.4 21.1 1.0
O4 A:PRP403 4.4 32.9 1.0
O1A A:PRP403 4.4 28.7 1.0
OD1 A:ASP251 4.5 21.6 1.0
CG A:ASP251 4.5 20.5 1.0
C A:VAL106 4.6 18.0 1.0
C1 A:PRP403 4.6 31.7 1.0
CA A:VAL106 4.9 18.6 1.0

Magnesium binding site 3 out of 4 in 4owu

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Magnesium binding site 3 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, 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-Methylanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:21.9
occ:1.00
 O3B B:PRP403 2.0 19.9 1.0
O1A B:PRP403 2.0 25.3 1.0
OG B:SER119 2.0 18.4 1.0
OE2 B:GLU252 2.1 21.7 1.0
O B:HOH603 2.1 20.8 1.0
O B:HOH610 2.2 18.9 1.0
CB B:SER119 3.0 17.6 1.0
CD B:GLU252 3.1 23.7 1.0
PA B:PRP403 3.2 25.4 1.0
PB B:PRP403 3.3 21.9 1.0
OE1 B:GLU252 3.3 24.5 1.0
MG B:MG402 3.4 30.0 1.0
O3A B:PRP403 3.5 26.9 1.0
O B:HOH657 3.9 23.4 1.0
N B:SER119 4.0 18.1 1.0
N B:GLY107 4.0 20.4 1.0
OD2 B:ASP251 4.0 22.9 1.0
CA B:SER119 4.1 17.8 1.0
O1B B:PRP403 4.3 22.0 1.0
O B:ASP251 4.3 21.4 1.0
O1 B:PRP403 4.3 29.6 1.0
O2B B:PRP403 4.3 20.9 1.0
O4 B:PRP403 4.3 33.6 1.0
O2A B:PRP403 4.4 28.6 1.0
O B:HOH737 4.4 22.0 1.0
CA B:GLY107 4.4 20.5 1.0
CG B:GLU252 4.4 23.5 1.0
OD1 B:ASP251 4.5 23.7 1.0
CG B:ASP251 4.5 23.6 1.0
C1 B:PRP403 4.6 32.6 1.0
C B:VAL106 4.7 20.1 1.0
CA B:VAL106 4.9 19.3 1.0

Magnesium binding site 4 out of 4 in 4owu

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Magnesium binding site 4 out of 4 in the Anthranilate Phosphoribosyl Transferase From Mycobacterium Tuberculosis in Complex with 5-Methylanthranilate, 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-Methylanthranilate, Prpp and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:30.0
occ:1.00
 OE2 B:GLU252 2.3 21.7 1.0
OD1 B:ASP251 2.4 23.7 1.0
O B:HOH738 2.4 38.9 1.0
O B:HOH603 2.5 20.8 1.0
O B:HOH657 2.5 23.4 1.0
CD B:GLU252 3.2 23.7 1.0
CG B:ASP251 3.3 23.6 1.0
CG B:GLU252 3.4 23.5 1.0
MG B:MG401 3.4 21.9 1.0
OD2 B:ASP251 3.6 22.9 1.0
O3B B:PRP403 3.7 19.9 1.0
O B:HOH644 3.8 34.7 1.0
OD2 B:ASP111 3.9 35.7 1.0
O B:HOH734 4.2 33.8 1.0
O B:HOH610 4.3 18.9 1.0
OG1 B:THR115 4.3 29.7 1.0
O B:ASP251 4.3 21.4 1.0
OE1 B:GLU252 4.4 24.5 1.0
C B:ASP251 4.6 23.3 1.0
CB B:ASP251 4.7 23.2 1.0
CG B:ASP111 4.7 35.1 1.0
N B:ASP251 4.8 24.7 1.0
O1B B:PRP403 4.8 22.0 1.0
PB B:PRP403 4.8 21.9 1.0
CB B:GLU252 4.8 23.3 1.0
O4 B:PRP403 4.9 33.6 1.0
CA B:ASP251 4.9 23.5 1.0
O1A B:PRP403 5.0 25.3 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 01:01:45 2024

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