Magnesium in PDB 2j0w: Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State)

Enzymatic activity of Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State)

All present enzymatic activity of Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State):
2.7.2.4;

Protein crystallography data

The structure of Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State), PDB code: 2j0w was solved by M.Kotaka, J.Ren, M.Lockyer, A.R.Hawkins, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	29.79 / 2.5
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	49.535, 213.347, 93.078, 90.00, 90.00, 90.00
*R / R_free (%)*	23.5 / 29.3

Other elements in 2j0w:

The structure of Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State) also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State) (pdb code 2j0w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State), PDB code: 2j0w:

Magnesium binding site 1 out of 1 in 2j0w

Go back to

Magnesium Binding Sites List in 2j0w

Magnesium binding site 1 out of 1 in the Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of E. Coli Aspartokinase III in Complex with Aspartate and Adp (R-State) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg900 b:41.1 occ:1.00	O	A:HOH2038	1.9	45.9	1.0
	O3B	A:ADP820	2.1	61.6	1.0
	O	A:HOH2067	2.2	47.8	1.0
	O	A:HOH2068	2.3	47.3	1.0
	O	A:HOH2039	2.5	34.8	1.0
	O2A	A:ADP820	2.6	47.2	1.0
	O	A:HOH2001	3.2	42.8	1.0
	PB	A:ADP820	3.4	54.2	1.0
	OD2	A:ASP202	3.6	40.8	1.0
	NZ	A:LYS8	3.8	37.8	1.0
	O2B	A:ADP820	3.8	57.2	1.0
	PA	A:ADP820	3.9	48.6	1.0
	CA	A:GLY199	3.9	39.6	1.0
	OD2	A:ASP502	3.9	53.0	1.0
	O3A	A:ADP820	4.0	40.3	1.0
	O	A:GLY199	4.2	42.8	1.0
	OD1	A:ASP502	4.3	40.3	1.0
	CG	A:ASP202	4.3	45.5	1.0
	CG	A:ASP502	4.5	49.9	1.0
	C	A:GLY199	4.5	41.0	1.0
	OD1	A:ASP202	4.5	41.4	1.0
	O1B	A:ADP820	4.6	58.1	1.0
	O5'	A:ADP820	4.7	49.0	1.0
	O	A:LYS257	4.7	40.1	1.0
	N	A:GLY199	5.0	43.1	1.0

Reference:

M.Kotaka, J.Ren, M.Lockyer, A.R.Hawkins, D.K.Stammers. Structures of R- and T-State Escherichia Coli Aspartokinase III: Mechanisms of the Allosteric Transition and Inhibition By Lysine. J.Biol.Chem. V. 281 31544 2006.
ISSN: ISSN 0021-9258
PubMed: 16905770
DOI: 10.1074/JBC.M605886200

Page generated: Mon Dec 14 07:28:10 2020

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