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Sodium in PDB 5jei: Crystal Structure of the GLUA2 Lbd in Complex with Fw

Protein crystallography data

The structure of Crystal Structure of the GLUA2 Lbd in Complex with Fw, PDB code: 5jei was solved by C.Eibl, H.Salazar, M.Chebli, A.J.R.Plested, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.37 / 1.23
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 126.465, 44.425, 47.276, 90.00, 90.00, 90.00
R / Rfree (%) 12.1 / 14.7

Other elements in 5jei:

The structure of Crystal Structure of the GLUA2 Lbd in Complex with Fw also contains other interesting chemical elements:

Fluorine (F) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the GLUA2 Lbd in Complex with Fw (pdb code 5jei). 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 GLUA2 Lbd in Complex with Fw, PDB code: 5jei:

Sodium binding site 1 out of 1 in 5jei

Go back to Sodium Binding Sites List in 5jei
Sodium binding site 1 out of 1 in the Crystal Structure of the GLUA2 Lbd in Complex with Fw


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 GLUA2 Lbd in Complex with Fw within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na314

b:39.6
occ:1.00
OE1 A:GLU198 3.1 19.0 1.0
CD A:GLU198 3.7 15.0 1.0
O A:HOH740 3.8 33.2 1.0
OE2 A:GLU198 3.8 16.6 1.0
O A:HOH406 3.9 26.2 1.0
O A:HOH596 4.0 28.4 1.0
O A:HOH502 4.0 13.5 1.0
O A:HOH465 4.1 17.7 1.0
OH A:TYR256 4.1 15.0 1.0
HH A:TYR256 4.1 18.0 1.0
HZ1 A:LYS251 4.1 17.3 1.0
O A:HOH422 4.2 16.6 1.0
O A:HOH771 4.4 38.2 1.0
HZ3 A:LYS251 4.5 17.3 1.0
NZ A:LYS251 4.7 14.4 1.0
O A:HOH478 4.7 19.6 1.0
O A:HOH559 4.8 31.9 1.0
HZ2 A:LYS251 4.9 17.3 1.0
CG A:GLU198 5.0 12.0 1.0

Reference:

H.Salazar, C.Eibl, M.Chebli, A.Plested. Mechanism of Partial Agonism in Ampa-Type Glutamate Receptors. Nat Commun V. 8 14327 2017.
ISSN: ESSN 2041-1723
PubMed: 28211453
DOI: 10.1038/NCOMMS14327
Page generated: Mon Oct 7 21:52:54 2024

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