Sodium 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:

Magnesium

(Mg)

1 atom

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer to 2.6 A, PDB code: 6h92:

Sodium binding site 1 out of 1 in 6h92

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Sodium Binding Sites List in 6h92

Sodium 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 Sodium with other atoms in the Na 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
B:Na301 b:35.5 occ:1.00	OP2	B:PHD8	2.4	29.4	1.0
	OD1	B:ASP170	2.5	39.6	1.0
	O	B:ASP10	2.6	34.6	1.0
	OD2	B:ASP10	3.2	43.9	1.0
	OD2	B:PHD8	3.2	33.2	1.0
	CG	B:ASP170	3.4	39.4	1.0
	C	B:ASP10	3.6	33.1	1.0
	OD2	B:ASP170	3.6	39.6	1.0
	CG	B:ASP10	3.9	42.6	1.0
	P	B:PHD8	3.9	31.8	1.0
	CB	B:ASP10	3.9	38.9	1.0
	CG	B:PHD8	4.2	32.1	1.0
	CA	B:ASP10	4.3	34.6	1.0
	OG	B:SER171	4.4	37.7	1.0
	N	B:GLY11	4.5	31.1	1.0
	OD1	B:PHD8	4.5	31.6	1.0
	OE1	B:GLU169	4.7	41.9	1.0
	CA	B:GLY11	4.7	28.6	1.0
	CB	B:SER171	4.7	37.5	1.0
	OP1	B:PHD8	4.7	35.2	1.0
	CB	B:ASP170	4.8	38.0	1.0
	OP3	B:PHD8	4.9	30.8	1.0
	N	B:ASP10	4.9	33.1	1.0
	OD1	B:ASP10	4.9	46.2	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: Tue Oct 8 09:15:35 2024

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