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 / R_free (%)*	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

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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

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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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