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Magnesium in PDB 5byt: Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd)

Enzymatic activity of Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd)

All present enzymatic activity of Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd):
2.4.2.18;

Protein crystallography data

The structure of Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd), PDB code: 5byt was solved by G.L.Evans, E.N.Baker, J.S.Lott, Tb Structural Genomics Consortium(Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.29 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 112.011, 81.192, 78.578, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd) (pdb code 5byt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd), PDB code: 5byt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5byt

Go back to Magnesium Binding Sites List in 5byt
Magnesium binding site 1 out of 2 in the Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:15.7
occ:1.00
 O A:HOH533 2.0 13.2 1.0
OE2 A:GLU252 2.0 13.9 1.0
O1A A:PRP402 2.0 14.6 1.0
O1B A:PRP402 2.1 13.3 1.0
OG A:SER119 2.2 12.5 1.0
O A:HOH505 2.3 14.2 1.0
CB A:SER119 3.0 8.6 1.0
CD A:GLU252 3.0 13.9 1.0
PA A:PRP402 3.1 14.7 1.0
PB A:PRP402 3.1 16.5 1.0
O3A A:PRP402 3.3 23.6 1.0
OE1 A:GLU252 3.4 13.0 1.0
O A:HOH511 3.4 15.3 1.0
N A:GLY107 3.9 13.9 1.0
OD2 A:ASP251 4.0 12.3 1.0
O2A A:PRP402 4.0 19.1 1.0
O A:HOH583 4.0 14.8 1.0
O4 A:PRP402 4.0 22.4 1.0
O3B A:PRP402 4.1 11.4 1.0
N A:SER119 4.1 9.4 1.0
O2B A:PRP402 4.1 22.9 1.0
CA A:SER119 4.1 10.8 1.0
O A:HOH663 4.2 13.3 1.0
O1 A:PRP402 4.3 21.1 1.0
O A:ASP251 4.3 10.0 1.0
CA A:GLY107 4.3 16.6 1.0
CG A:GLU252 4.4 15.4 1.0
CG A:ASP251 4.5 13.0 1.0
C1 A:PRP402 4.5 19.3 1.0
O A:HOH639 4.5 22.4 1.0
OD1 A:ASP251 4.5 18.8 1.0
C A:VAL106 4.6 15.9 1.0
CA A:VAL106 4.9 12.3 1.0

Magnesium binding site 2 out of 2 in 5byt

Go back to Magnesium Binding Sites List in 5byt
Magnesium binding site 2 out of 2 in the Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Prpp Complexed with A Single Mg in the Active Site of Mycobacterium Tuberculosis Anthranilate Phosphoribosyltransferase (Anprt; Trpd) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:18.1
occ:1.00
 O1A B:PRP402 2.0 19.3 0.6
OE2 B:GLU252 2.0 20.5 1.0
OG B:SER119 2.1 17.2 1.0
O B:HOH549 2.2 14.0 1.0
O2B B:PRP402 2.2 20.2 0.6
O2B B:PRP402 2.3 20.4 0.4
O B:HOH508 2.3 23.2 0.9
O1A B:PRP402 2.3 18.5 0.4
CB B:SER119 3.0 15.0 1.0
CD B:GLU252 3.0 19.9 1.0
PA B:PRP402 3.2 20.3 0.6
PB B:PRP402 3.3 23.1 0.6
PA B:PRP402 3.4 20.1 0.4
OE1 B:GLU252 3.4 23.6 1.0
PB B:PRP402 3.5 22.6 0.4
O3A B:PRP402 3.5 24.1 0.6
O1 B:PRP402 3.8 20.5 0.4
O B:HOH542 3.8 24.0 1.0
O B:HOH530 3.8 18.5 1.0
O3A B:PRP402 3.8 24.2 0.4
O2A B:PRP402 3.9 24.3 0.6
N B:GLY107 3.9 17.4 1.0
N B:SER119 4.1 14.1 1.0
OD2 B:ASP251 4.1 21.3 1.0
CA B:SER119 4.1 15.9 1.0
O1B B:PRP402 4.2 21.8 0.6
O4 B:PRP402 4.3 22.4 0.6
O1B B:PRP402 4.3 21.8 0.4
O B:ASP251 4.3 15.3 1.0
CA B:GLY107 4.3 19.6 1.0
CG B:GLU252 4.3 19.7 1.0
O3B B:PRP402 4.4 21.6 0.6
O1 B:PRP402 4.4 20.8 0.6
O B:HOH575 4.4 17.2 1.0
C B:VAL106 4.5 15.9 1.0
O3B B:PRP402 4.5 21.9 0.4
O2A B:PRP402 4.6 23.4 0.4
C1 B:PRP402 4.6 22.7 0.6
CG B:ASP251 4.6 23.2 1.0
OD1 B:ASP251 4.7 27.5 1.0
CA B:VAL106 4.7 18.6 1.0
O3 B:PRP402 4.9 21.8 0.4

Reference:

G.L.Evans, E.N.Baker, J.S.Lott. Binding and Mimicking of the Phosphate-Rich Substrate, Prpp. To Be Published.
Page generated: Sun Sep 29 01:49:20 2024

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