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Sodium in PDB 6fsq: Structure of A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd)

Protein crystallography data

The structure of Structure of A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd), PDB code: 6fsq was solved by I.Li De La Sierra-Gallay, C.Leger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.51 / 2.79
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.940, 89.030, 143.610, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 27

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd) (pdb code 6fsq). 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 A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd), PDB code: 6fsq:

Sodium binding site 1 out of 1 in 6fsq

Go back to Sodium Binding Sites List in 6fsq
Sodium binding site 1 out of 1 in the Structure of A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of A3_BGFPD, An Artificial Bi-Domain Protein Based on Two Different Alpharep Domains : A3 and A Gfp Binding Domain (Bgfpd) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na502

b:41.8
occ:1.00
CD A:ARG72 3.3 69.3 1.0
NH2 A:ARG72 3.4 90.5 1.0
CE2 A:TRP69 3.8 43.0 1.0
CZ2 A:TRP69 3.9 45.3 1.0
N A:ALA73 3.9 52.6 1.0
CB A:ALA73 4.0 49.2 1.0
CH2 A:TRP69 4.0 45.1 1.0
CD2 A:TRP69 4.0 43.4 1.0
CA A:ALA73 4.0 49.0 1.0
CB A:ARG72 4.1 57.9 1.0
CZ3 A:TRP69 4.1 43.9 1.0
CE3 A:TRP69 4.2 44.3 1.0
NE A:ARG72 4.2 76.5 1.0
CZ A:ARG72 4.2 81.8 1.0
CG A:ARG72 4.3 63.9 1.0
O A:TRP69 4.3 50.9 1.0
NE1 A:TRP69 4.4 42.1 1.0
C A:ARG72 4.5 50.1 1.0
CG A:TRP69 4.6 43.9 1.0
CD1 A:TRP69 4.8 43.6 1.0

Reference:

C.Leger, T.Di Meo, M.Aumont-Nicaise, C.Velours, D.Durand, I.Li De La Sierra-Gallay, H.Van Tilbeurgh, N.Hildebrandt, M.Desmadril, A.Urvoas, M.Valerio-Lepiniec, P.Minard. Ligand-Induced Conformational Switch in An Artificial Bidomain Protein Scaffold. Sci Rep V. 9 1178 2019.
ISSN: ESSN 2045-2322
PubMed: 30718544
DOI: 10.1038/S41598-018-37256-5
Page generated: Tue Oct 8 08:49:47 2024

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