Magnesium in PDB 6n4l: Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii

Enzymatic activity of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii

All present enzymatic activity of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii, PDB code: 6n4l was solved by B.B.Wenke, T.Spatzal, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	39.04 / 1.13
*Space group*	P 2 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	45.587, 74.630, 75.398, 90.00, 90.00, 90.00
*R / R_free (%)*	14.6 / 15.7

Other elements in 6n4l:

The structure of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii (pdb code 6n4l). 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 Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii, PDB code: 6n4l:

Magnesium binding site 1 out of 1 in 6n4l

Go back to

Magnesium Binding Sites List in 6n4l

Magnesium binding site 1 out of 1 in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg302 b:9.8 occ:1.00	O	A:HOH440	2.0	10.6	1.0
	O3B	A:ADP301	2.0	9.6	1.0
	OG	A:SER16	2.1	9.6	1.0
	O	A:HOH480	2.1	11.8	1.0
	O	A:HOH436	2.1	11.2	1.0
	O	A:HOH473	2.1	11.5	1.0
	CB	A:SER16	3.1	9.5	1.0
	PB	A:ADP301	3.3	9.7	1.0
	O1B	A:ADP301	3.6	10.2	1.0
	OD2	A:ASP39	3.7	11.2	1.0
	OD1	A:ASP43	3.9	17.4	1.0
	N	A:SER16	3.9	9.0	1.0
	OD2	A:ASP125	4.1	10.6	1.0
	CA	A:SER16	4.1	9.5	1.0
	O1A	A:ADP301	4.1	11.4	1.0
	OG	A:SER44	4.2	12.2	1.0
	O3A	A:ADP301	4.3	10.4	1.0
	OD1	A:ASP125	4.3	10.0	1.0
	O2B	A:ADP301	4.3	9.6	1.0
	CG	A:ASP39	4.5	10.1	1.0
	PA	A:ADP301	4.6	10.8	1.0
	O	A:HOH555	4.6	23.6	1.0
	CG	A:ASP125	4.6	9.2	1.0
	O2A	A:ADP301	4.7	11.1	1.0
	CB	A:ASP39	4.8	10.1	1.0
	CB	A:LYS15	4.9	9.4	1.0
	CE	A:LYS15	4.9	10.0	1.0

Reference:

B.B.Wenke, T.Spatzal, D.C.Rees. Site-Specific Oxidation State Assignments of the Iron Atoms in the [4FE:4S]2+/1+/0STATES of the Nitrogenase Fe-Protein. Angew. Chem. Int. Ed. Engl. V. 58 3894 2019.
ISSN: ESSN 1521-3773
PubMed: 30698901
DOI: 10.1002/ANIE.201813966

Page generated: Tue Oct 1 12:25:41 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy