Magnesium in PDB 4x59: Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg

All present enzymatic activity of Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg:
2.4.2.18;

The structure of Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x59 was solved by T.V.M.Cookson, G.L.Evans, E.J.Parker, J.S.Lott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.21 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.234, 78.339, 102.155, 90.00, 111.74, 90.00
R / Rfree (%)	19 / 22

The binding sites of Magnesium atom in the Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg (pdb code 4x59). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x59:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:16.4 occ:1.00 O1B B:PRP401 2.0 19.2 0.8 O1B B:PRP401 2.0 16.5 0.2 O1A B:PRP401 2.0 22.0 0.8 O B:HOH627 2.1 19.8 1.0 OE1 B:GLU252 2.1 19.5 1.0 OG B:SER119 2.2 15.8 1.0 O B:HOH628 2.2 18.5 1.0 O1A B:PRP401 2.4 17.0 0.2 CD B:GLU252 3.0 19.7 1.0 OE2 B:GLU252 3.1 19.8 1.0 CB B:SER119 3.2 16.5 1.0 PA B:PRP401 3.2 22.1 0.8 MG B:MG403 3.3 29.4 1.0 PB B:PRP401 3.3 17.0 0.2 PB B:PRP401 3.3 21.8 0.8 O3A B:PRP401 3.5 16.6 0.2 PA B:PRP401 3.5 16.7 0.2 O3A B:PRP401 3.5 22.4 0.8 O B:HOH629 3.7 38.5 1.0 O1 B:PRP401 3.8 24.9 0.8 OD2 B:ASP251 4.0 20.1 1.0 N B:SER119 4.0 16.7 1.0 O3B B:PRP401 4.1 16.7 0.2 N B:GLY107 4.1 17.2 1.0 O B:ASP251 4.1 16.6 1.0 CA B:SER119 4.2 16.9 1.0 O B:HOH557 4.2 22.8 1.0 O3B B:PRP401 4.2 21.6 0.8 OD1 B:ASP251 4.3 20.3 1.0 O2B B:PRP401 4.4 20.8 0.8 CG B:GLU252 4.4 19.7 1.0 CG B:ASP251 4.4 19.9 1.0 CA B:GLY107 4.4 16.0 1.0 O4 B:PRP401 4.4 16.5 0.2 O2B B:PRP401 4.4 16.9 0.2 O2A B:PRP401 4.5 23.2 0.8 O1 B:PRP401 4.5 16.9 0.2 C B:VAL106 4.6 16.9 1.0 O3 B:PRP401 4.7 30.9 0.8 O2A B:PRP401 4.7 16.9 0.2 O B:HOH603 4.9 23.1 1.0 C4 B:PRP401 4.9 16.4 0.2 CA B:VAL106 4.9 16.4 1.0 O B:HOH630 5.0 28.4 1.0

Magnesium binding site 2 out of 2 in the Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Anthranilate Phosphoribosyltransferase Variant P180A From Mycobacterium Tuberculosis in Complex with Prpp and Mg within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:29.4 occ:1.00 O B:HOH629 2.1 38.5 1.0 O B:HOH630 2.1 28.4 1.0 OE1 B:GLU252 2.2 19.5 1.0 OD1 B:ASP251 2.2 20.3 1.0 O B:HOH628 2.3 18.5 1.0 O B:HOH631 2.3 29.7 1.0 CG B:ASP251 3.2 19.9 1.0 CD B:GLU252 3.2 19.7 1.0 MG B:MG402 3.3 16.4 1.0 OD2 B:ASP251 3.4 20.1 1.0 CG B:GLU252 3.6 19.7 1.0 O1B B:PRP401 3.6 19.2 0.8 O1B B:PRP401 3.7 16.5 0.2 OD2 B:ASP111 3.8 33.8 1.0 O B:HOH632 3.9 39.1 1.0 O B:ASP251 4.2 16.6 1.0 O3 B:PRP401 4.2 30.9 0.8 O B:HOH627 4.2 19.8 1.0 OG1 B:THR115 4.3 33.2 1.0 OE2 B:GLU252 4.3 19.8 1.0 C4 B:PRP401 4.5 16.4 0.2 CB B:ASP251 4.5 19.8 1.0 C B:ASP251 4.6 18.4 1.0 O3B B:PRP401 4.6 21.6 0.8 PB B:PRP401 4.7 21.8 0.8 CG B:ASP111 4.7 36.5 1.0 O1A B:PRP401 4.8 17.0 0.2 N B:ASP251 4.8 20.0 1.0 O1A B:PRP401 4.8 22.0 0.8 O3B B:PRP401 4.8 16.7 0.2 PB B:PRP401 4.9 17.0 0.2 CA B:ASP251 4.9 19.1 1.0 O4 B:PRP401 4.9 16.5 0.2

T.V.Cookson, G.L.Evans, A.Castell, E.N.Baker, J.S.Lott, E.J.Parker. Structures of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site. Biochemistry V. 54 6082 2015.
ISSN: ISSN 0006-2960
PubMed: 26356348
DOI: 10.1021/ACS.BIOCHEM.5B00612