Sodium in PDB 3fl7: Crystal Structure of the Human Ephrin A2 Ectodomain

All present enzymatic activity of Crystal Structure of the Human Ephrin A2 Ectodomain:
2.7.10.1;

The structure of Crystal Structure of the Human Ephrin A2 Ectodomain, PDB code: 3fl7 was solved by J.R.Walker, L.Yermekbayeva, A.Seitova, C.Butler-Cole, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, S.Dhe-Paganon, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.59 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.358, 89.992, 136.476, 90.00, 90.00, 90.00
R / Rfree (%)	24.6 / 29.9

The structure of Crystal Structure of the Human Ephrin A2 Ectodomain also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Sodium atom in the Crystal Structure of the Human Ephrin A2 Ectodomain (pdb code 3fl7). 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 Human Ephrin A2 Ectodomain, PDB code: 3fl7:

Sodium binding site 1 out of 1 in the Crystal Structure of the Human Ephrin A2 Ectodomain


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 Human Ephrin A2 Ectodomain within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1001 b:48.8 occ:1.00 OD2 A:ASP148 2.2 84.6 1.0 OE2 A:GLU166 2.2 76.8 1.0 CG A:ASP148 3.1 83.9 1.0 OD1 A:ASP148 3.3 84.0 1.0 CD A:GLU166 3.3 72.4 1.0 OE1 A:GLU166 3.7 72.3 1.0 O A:ALA146 4.3 68.0 1.0 CB A:ASP148 4.5 84.4 1.0 CG A:GLU166 4.6 69.3 1.0 N A:ASP148 4.8 78.9 1.0 CA A:ASP148 4.9 83.0 1.0

J.P.Himanen, L.Yermekbayeva, P.W.Janes, J.R.Walker, K.Xu, L.Atapattu, K.R.Rajashankar, A.Mensinga, M.Lackmann, D.B.Nikolov, S.Dhe-Paganon. Architecture of Eph Receptor Clusters. Proc.Natl.Acad.Sci.Usa V. 107 10860 2010.
ISSN: ISSN 0027-8424
PubMed: 20505120
DOI: 10.1073/PNAS.1004148107