Sodium in PDB 2gmh: Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone

Enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone

All present enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone:
1.5.5.1;

Protein crystallography data

The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh was solved by J.Zhang, F.E.Frerman, J.-J.P.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	29.67 / 2.50
*Space group*	P 4 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	154.322, 154.322, 128.536, 90.00, 90.00, 90.00
*R / R_free (%)*	22.1 / 25.4

Other elements in 2gmh:

The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone (pdb code 2gmh). 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 Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh:

Sodium binding site 1 out of 1 in 2gmh

Go back to

Sodium Binding Sites List in 2gmh

Sodium binding site 1 out of 1 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na1070 b:37.5 occ:1.00	O	A:HOH966	2.3	36.3	1.0
	O	A:HOH944	2.5	32.2	1.0
	O	A:HOH935	2.5	24.6	1.0
	O	A:HOH828	2.7	31.2	1.0
	O	A:ASN232	2.7	27.1	1.0
	O	A:HOH874	2.7	38.9	1.0
	C	A:ASN232	3.9	26.0	1.0
	O	A:HOH801	4.1	14.1	1.0
	O	A:HOH986	4.1	22.9	1.0
	O	A:HOH995	4.1	38.7	1.0
	CA	A:CYS233	4.1	28.0	1.0
	CB	A:CYS233	4.2	27.1	1.0
	O	A:GLN339	4.4	24.8	1.0
	O	A:HOH842	4.5	32.4	1.0
	N	A:CYS233	4.5	25.4	1.0
	O	A:HOH996	4.6	43.1	1.0
	O	A:HOH897	4.6	46.2	1.0
	CB	A:ASN232	4.7	27.7	1.0
	O	A:ILE341	4.8	23.3	1.0
	CA	A:ASN232	4.9	27.0	1.0

Reference:

J.Zhang, F.E.Frerman, J.J.Kim. Structure of Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase and Electron Transfer to the Mitochondrial Ubiquinone Pool. Proc.Natl.Acad.Sci.Usa V. 103 16212 2006.
ISSN: ISSN 0027-8424
PubMed: 17050691
DOI: 10.1073/PNAS.0604567103

Page generated: Tue Dec 15 05:49:58 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3

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