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Sodium in PDB 3us3: Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex

Protein crystallography data

The structure of Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex, PDB code: 3us3 was solved by E.J.Sanchez, K.M.Lewis, M.S.Nissen, G.R.Munske, C.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.91 / 1.74
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 59.214, 144.811, 110.471, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 23.2

Other elements in 3us3:

The structure of Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex (pdb code 3us3). 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 Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex, PDB code: 3us3:

Sodium binding site 1 out of 1 in 3us3

Go back to Sodium Binding Sites List in 3us3
Sodium binding site 1 out of 1 in the Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Recombinant Rabbit Skeletal Calsequestrin-Mpd Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na376

b:44.2
occ:1.00
O A:PRO172 2.0 24.4 1.0
O A:HOH629 2.5 39.6 1.0
O A:HOH771 2.8 42.4 1.0
C A:PRO172 3.2 19.1 1.0
O A:HOH603 3.8 34.1 1.0
O A:TYR173 4.0 22.3 1.0
C A:TYR173 4.0 27.7 1.0
CA A:TYR173 4.0 20.1 1.0
N A:TYR173 4.1 20.1 1.0
CB A:PRO172 4.2 19.4 1.0
CA A:PRO172 4.2 18.2 1.0
OE1 A:GLU145 4.3 44.3 1.0
OD1 A:ASP121 4.6 31.1 1.0
OE2 A:GLU236 4.6 42.7 1.0
N A:ILE174 4.7 20.6 1.0
O A:HOH657 4.7 42.5 1.0
OE1 A:GLU236 4.8 47.3 1.0
CG A:PRO172 4.8 18.9 1.0
O A:HOH476 4.9 26.6 1.0
CG A:ASP121 4.9 30.0 1.0
CD A:PRO175 4.9 18.8 1.0

Reference:

E.J.Sanchez, K.M.Lewis, G.R.Munske, M.S.Nissen, C.Kang. Glycosylation of Skeletal Calsequestrin: Implications For Its Function. J.Biol.Chem. V. 287 3042 2012.
ISSN: ISSN 0021-9258
PubMed: 22170046
DOI: 10.1074/JBC.M111.326363
Page generated: Tue Dec 15 06:27:37 2020

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