Magnesium in PDB 1kh9: E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate

Enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate:
3.1.3.1;

Protein crystallography data

The structure of E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate, PDB code: 1kh9 was solved by M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 2.50
*Space group*	P 6₃ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	164.010, 164.010, 138.878, 90.00, 90.00, 120.00
*R / R_free (%)*	19.6 / 25

Other elements in 1kh9:

The structure of E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate (pdb code 1kh9). 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 E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate, PDB code: 1kh9:

Magnesium binding site 1 out of 1 in 1kh9

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Magnesium Binding Sites List in 1kh9

Magnesium binding site 1 out of 1 in the E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Alkaline Phosphatase Mutant (D153GD330N) Complex with Phosphate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg452 b:38.5 occ:1.00	OE2	A:GLU322	2.0	25.5	1.0
	OD1	A:ASP51	2.2	37.8	1.0
	OG1	A:THR155	2.3	24.1	1.0
	CG	A:ASP51	3.1	36.8	1.0
	CD	A:GLU322	3.3	28.9	1.0
	OD2	A:ASP51	3.5	33.5	1.0
	CB	A:THR155	3.6	13.0	1.0
	OE1	A:GLU322	4.0	32.4	1.0
	CG	A:GLU322	4.2	18.5	1.0
	CB	A:ASP51	4.3	27.6	1.0
	N	A:THR155	4.3	7.7	1.0
	O	A:HOH1107	4.3	28.0	1.0
	CG2	A:THR155	4.6	12.9	1.0
	CB	A:ALA324	4.6	19.9	1.0
	CA	A:THR155	4.6	9.8	1.0
	CA	A:ALA324	4.7	19.1	1.0
	O	A:ALA324	4.8	25.0	1.0
	OD1	A:ASP369	4.9	26.2	1.0
	ZN	A:ZN451	5.0	50.0	1.0
	CB	A:SER102	5.0	16.9	1.0

Reference:

M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, A.Menez, J.C.Boulain. Artificial Evolution of An Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 316 941 2002.
ISSN: ISSN 0022-2836
PubMed: 11884134
DOI: 10.1006/JMBI.2001.5384

Page generated: Sun Aug 10 00:10:19 2025

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