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Magnesium in PDB 4x58: Anthranilate Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg

Enzymatic activity of Anthranilate Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg

All present enzymatic activity of Anthranilate Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg:
2.4.2.18;

Protein crystallography data

The structure of Anthranilate Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x58 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) 94.41 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 94.739, 78.067, 101.331, 90.00, 111.30, 90.00
R / Rfree (%) 19.5 / 22.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Anthranilate Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg (pdb code 4x58). 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 Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg, PDB code: 4x58:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4x58

Go back to Magnesium Binding Sites List in 4x58
Magnesium binding site 1 out of 2 in the Anthranilate Phosphoribosyl Transferase Variant N138A 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 Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg406

b:27.7
occ:1.00
O A:HOH633 2.0 23.8 1.0
OE1 A:GLU252 2.1 13.4 1.0
O A:HOH634 2.2 29.5 1.0
O A:HOH632 2.3 28.0 1.0
O A:HOH629 2.4 15.3 1.0
OD1 A:ASP251 2.4 14.5 1.0
CD A:GLU252 3.2 13.4 1.0
MG A:MG407 3.3 15.1 1.0
CG A:ASP251 3.4 14.4 1.0
CG A:GLU252 3.5 13.7 1.0
O3B A:PRP405 3.6 17.3 1.0
OD2 A:ASP251 3.6 14.2 1.0
OD2 A:ASP111 3.7 26.4 1.0
OG1 A:THR115 4.3 22.3 1.0
O A:HOH631 4.3 9.8 1.0
OE2 A:GLU252 4.3 13.3 1.0
O A:ASP251 4.3 12.9 1.0
O1B A:PRP405 4.5 18.8 1.0
C A:ASP251 4.6 13.7 1.0
PB A:PRP405 4.6 18.6 1.0
O4 A:PRP405 4.6 23.6 1.0
CB A:ASP251 4.7 14.2 1.0
CG A:ASP111 4.7 24.6 1.0
N A:ASP251 4.8 14.8 1.0
CA A:ASP251 4.9 14.1 1.0
CB A:GLU252 4.9 13.7 1.0
O2A A:PRP405 4.9 18.4 1.0

Magnesium binding site 2 out of 2 in 4x58

Go back to Magnesium Binding Sites List in 4x58
Magnesium binding site 2 out of 2 in the Anthranilate Phosphoribosyl Transferase Variant N138A 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 Phosphoribosyl Transferase Variant N138A From Mycobacterium Tuberculosis in Complex with Prpp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg407

b:15.1
occ:1.00
O3B A:PRP405 2.0 17.3 1.0
O2A A:PRP405 2.1 18.4 1.0
O A:HOH631 2.1 9.8 1.0
O A:HOH629 2.1 15.3 1.0
OE1 A:GLU252 2.1 13.4 1.0
OG A:SER119 2.2 12.8 1.0
CD A:GLU252 3.0 13.4 1.0
CB A:SER119 3.2 12.8 1.0
OE2 A:GLU252 3.2 13.3 1.0
PA A:PRP405 3.3 19.5 1.0
MG A:MG406 3.3 27.7 1.0
PB A:PRP405 3.3 18.6 1.0
O3A A:PRP405 3.5 19.4 1.0
O A:HOH632 3.9 28.0 1.0
OD2 A:ASP251 3.9 14.2 1.0
N A:GLY107 3.9 13.0 1.0
N A:SER119 4.0 12.8 1.0
O A:ASP251 4.1 12.9 1.0
CA A:SER119 4.2 12.6 1.0
O A:HOH565 4.2 16.3 1.0
O1B A:PRP405 4.3 18.8 1.0
O4 A:PRP405 4.3 23.6 1.0
O1 A:PRP405 4.3 21.0 1.0
CA A:GLY107 4.3 13.2 1.0
O2B A:PRP405 4.3 17.1 1.0
OD1 A:ASP251 4.3 14.5 1.0
CG A:ASP251 4.4 14.4 1.0
CG A:GLU252 4.4 13.7 1.0
O1A A:PRP405 4.5 20.9 1.0
C1 A:PRP405 4.6 22.4 1.0
C A:VAL106 4.6 13.3 1.0
CA A:VAL106 4.9 13.0 1.0
O A:HOH634 4.9 29.5 1.0

Reference:

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
Page generated: Tue Aug 20 14:04:25 2024

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