Sodium in PDB 6o08: Gluconobacter Ene-Reductase (Gluer)

Protein crystallography data

The structure of Gluconobacter Ene-Reductase (Gluer), PDB code: 6o08 was solved by S.E.Garfinkle, P.Jeffrey, T.K.Hyster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.99 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.695, 49.469, 156.223, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22.3

Other elements in 6o08:

The structure of Gluconobacter Ene-Reductase (Gluer) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Gluconobacter Ene-Reductase (Gluer) (pdb code 6o08). 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 Gluconobacter Ene-Reductase (Gluer), PDB code: 6o08:

Sodium binding site 1 out of 1 in 6o08

Go back to Sodium Binding Sites List in 6o08
Sodium binding site 1 out of 1 in the Gluconobacter Ene-Reductase (Gluer)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Gluconobacter Ene-Reductase (Gluer) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na411

b:63.2
occ:1.00
OXT A:ACT406 2.6 63.6 1.0
OH A:TYR343 3.1 36.7 1.0
CH3 A:ACT406 3.3 55.4 1.0
C A:ACT406 3.3 52.7 1.0
CH2 A:TRP66 3.7 40.5 1.0
N5 A:FMN401 3.8 33.2 1.0
CZ A:TYR343 3.8 37.2 1.0
C5A A:FMN401 3.8 30.6 1.0
CZ3 A:TRP66 3.9 40.8 1.0
CE1 A:TYR343 3.9 32.7 1.0
C6 A:FMN401 4.0 26.8 1.0
CB A:THR25 4.1 30.7 1.0
CZ2 A:TRP66 4.4 39.3 1.0
C4A A:FMN401 4.4 34.6 1.0
OG1 A:THR25 4.5 29.3 1.0
C9A A:FMN401 4.5 31.8 1.0
CG2 A:THR25 4.6 30.0 1.0
O A:ACT406 4.6 35.5 1.0
CE3 A:TRP66 4.6 40.7 1.0
OH A:TYR177 4.6 37.6 1.0
C7 A:FMN401 4.6 27.8 1.0
O A:HOH550 4.7 48.1 1.0
CE2 A:TYR343 4.9 35.3 1.0

Reference:

K.F.Biegasiewicz, S.J.Cooper, X.Gao, D.G.Oblinsky, J.H.Kim, S.E.Garfinkle, L.A.Joyce, B.A.Sandoval, G.D.Scholes, T.K.Hyster. Photoexcitation of Flavoenzymes Enables A Stereoselective Radical Cyclization. Science V. 364 1166 2019.
ISSN: ESSN 1095-9203
PubMed: 31221855
DOI: 10.1126/SCIENCE.AAW1143
Page generated: Tue Dec 15 12:40:44 2020

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