Sodium in PDB 3lo8: Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms

Enzymatic activity of Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms

All present enzymatic activity of Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms:
1.18.1.2;

Protein crystallography data

The structure of Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms, PDB code: 3lo8 was solved by H.R.Faber, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.05
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	59.140, 59.140, 186.740, 90.00, 90.00, 120.00
*R / R_free (%)*	12.5 / 15.5

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms (pdb code 3lo8). 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 Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms, PDB code: 3lo8:

Sodium binding site 1 out of 1 in 3lo8

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Sodium Binding Sites List in 3lo8

Sodium binding site 1 out of 1 in the Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Oxidized Form of Ferredoxin:Nadp+ Reductase From Maize Root at 1.05 Angstroms within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na1800 b:19.7 occ:1.00	O	A:HOH1194	2.0	24.3	1.0
	O	A:HOH1504	2.0	16.5	1.0
	O	A:HOH1517	2.0	23.1	1.0
	O	A:HOH1549	2.0	18.9	1.0
	O	A:HOH1510	2.1	23.7	1.0
	O	A:HOH1316	2.1	19.2	1.0
	HA	A:ASP211	3.8	22.4	1.0
	HB2	A:LEU213	4.0	17.1	1.0
	O	A:HOH1532	4.1	18.6	1.0
	O	A:SER210	4.1	17.9	1.0
	HA	A:VAL45	4.1	15.9	1.0
	O	A:HOH1384	4.2	35.6	1.0
	O	A:HOH1514	4.2	40.5	1.0
	O	A:HOH1303	4.3	34.3	1.0
	O	A:HOH1111	4.3	22.9	1.0
	O	A:ASP211	4.3	16.2	1.0
	O	A:LEU213	4.3	13.7	1.0
	O	A:HOH1355	4.3	25.6	1.0
	O	A:LEU44	4.3	13.9	1.0
	O	A:HOH1153	4.3	32.9	1.0
	H	A:GLY46	4.4	22.0	1.0
	CA	A:ASP211	4.6	18.7	1.0
	C	A:ASP211	4.6	16.9	1.0
	H	A:LEU213	4.7	16.4	1.0
	N	A:GLY46	4.8	18.3	1.0
	HA3	A:GLY46	4.9	23.6	1.0
	CB	A:LEU213	5.0	14.2	1.0

Reference:

D.E.Tronrud, D.S.Berkholz, P.A.Karplus. Using A Conformation-Dependent Stereochemical Library Improves Crystallographic Refinement of Proteins. Acta Crystallogr.,Sect.D V. 66 834 2010.
ISSN: ISSN 0907-4449
PubMed: 20606264
DOI: 10.1107/S0907444910019207

Page generated: Mon Oct 7 11:22:41 2024

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