Magnesium in PDB 6h92: Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A

Enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A

All present enzymatic activity of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A:
5.4.2.6;

Protein crystallography data

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A, PDB code: 6h92 was solved by A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	47.82 / 2.60
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	38.410, 117.180, 52.980, 90.00, 98.66, 90.00
*R / R_free (%)*	23.3 / 31.6

Other elements in 6h92:

The structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A (pdb code 6h92). 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 Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A, PDB code: 6h92:

Magnesium binding site 1 out of 1 in 6h92

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Magnesium Binding Sites List in 6h92

Magnesium binding site 1 out of 1 in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg301 b:31.1 occ:1.00	OD1	A:ASP170	1.9	39.0	1.0
	OP1	A:PHD8	2.3	27.3	1.0
	OD2	A:PHD8	2.3	32.3	1.0
	O	A:ASP10	2.3	30.8	1.0
	CG	A:ASP170	2.9	37.6	1.0
	OD2	A:ASP170	3.2	38.6	1.0
	CG	A:PHD8	3.4	31.2	1.0
	C	A:ASP10	3.5	31.3	1.0
	P	A:PHD8	3.7	30.4	1.0
	OE1	A:GLU169	3.7	46.8	1.0
	OD1	A:PHD8	3.9	30.4	1.0
	OG	A:SER171	4.1	36.0	1.0
	CB	A:ASP10	4.2	33.7	1.0
	CB	A:ASP170	4.3	36.6	1.0
	OD2	A:ASP10	4.3	34.1	1.0
	CA	A:ASP10	4.3	32.0	1.0
	N	A:ASP170	4.5	36.0	1.0
	N	A:GLY11	4.5	30.1	1.0
	O	A:HOH403	4.5	14.7	1.0
	N	A:ASP10	4.6	32.2	1.0
	CB	A:PHD8	4.6	31.3	1.0
	OP3	A:PHD8	4.6	30.1	1.0
	OP2	A:PHD8	4.6	29.8	1.0
	CG	A:ASP10	4.7	34.7	1.0
	CD	A:GLU169	4.7	42.6	1.0
	CB	A:SER171	4.7	36.1	1.0
	CA	A:GLY11	4.7	29.5	1.0
	CA	A:ASP170	4.8	36.1	1.0
	N	A:SER171	4.8	37.0	1.0
	C	A:ASP170	4.9	35.7	1.0

Reference:

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase To Be Published.

Page generated: Wed Aug 13 06:54:52 2025

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