Magnesium in PDB 4ehy: Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution

Enzymatic activity of Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution

All present enzymatic activity of Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution:
2.7.1.130;

Protein crystallography data

The structure of Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution, PDB code: 4ehy was solved by R.P.Emptage, K.D.Daughtry, C.W.Pemble Iv, C.R.H.Raetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	28.40 / 2.20
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	65.110, 75.610, 104.200, 90.00, 90.00, 90.00
*R / R_free (%)*	17.8 / 21.3

Other elements in 4ehy:

The structure of Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution (pdb code 4ehy). 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 Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution, PDB code: 4ehy:

Magnesium binding site 1 out of 1 in 4ehy

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Magnesium Binding Sites List in 4ehy

Magnesium binding site 1 out of 1 in the Crystal Structure of Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution

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 Lpxk From Aquifex Aeolicus in Complex with Adp/MG2+ at 2.2 Angstrom Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg403 b:61.3 occ:1.00	O	A:HOH504	2.0	64.1	1.0
	O	A:HOH503	2.1	61.9	1.0
	O1B	A:ADP401	2.1	59.0	1.0
	O	A:HOH502	2.1	64.5	1.0
	O	A:HOH501	2.1	51.2	1.0
	OE1	A:GLU100	2.2	59.6	1.0
	CD	A:GLU100	3.0	62.4	1.0
	OE2	A:GLU100	3.2	67.0	1.0
	PB	A:ADP401	3.6	48.3	1.0
	NZ	A:LYS51	4.1	55.1	1.0
	NZ	A:LYS280	4.2	41.1	1.0
	O2B	A:ADP401	4.2	65.4	1.0
	O2A	A:ADP401	4.2	45.7	1.0
	O	A:HOH505	4.3	51.5	1.0
	CE1	A:HIS261	4.3	47.4	1.0
	NE2	A:HIS261	4.3	47.0	1.0
	O3A	A:ADP401	4.4	48.9	1.0
	OD1	A:ASP260	4.4	51.5	1.0
	CG	A:GLU100	4.4	57.0	1.0
	O3B	A:ADP401	4.4	43.8	1.0
	O	A:HOH552	4.7	67.9	1.0
	CE	A:LYS51	4.7	62.3	1.0
	PA	A:ADP401	4.8	49.9	1.0
	OG1	A:THR52	4.8	42.2	1.0

Reference:

R.P.Emptage, K.D.Daughtry, C.W.Pemble, C.R.Raetz. Crystal Structure of Lpxk, the 4'-Kinase of Lipid A Biosynthesis and Atypical P-Loop Kinase Functioning at the Membrane Interface. Proc.Natl.Acad.Sci.Usa V. 109 12956 2012.
ISSN: ISSN 0027-8424
PubMed: 22826246
DOI: 10.1073/PNAS.1206072109

Page generated: Mon Dec 14 14:07:17 2020

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