Sodium in PDB 8trs: Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form

All present enzymatic activity of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form:
2.7.10.1;

The structure of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form, PDB code: 8trs was solved by A.U.Singer, H.A.Bruce, L.Blazer, J.J.Adams, F.Sicheri, S.S.Sidhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	61.81 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.376, 71.376, 235.014, 90, 90, 120
R / Rfree (%)	18 / 21.4

The structure of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form also contains other interesting chemical elements:

Chlorine

(Cl)

18 atoms

The binding sites of Sodium atom in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form (pdb code 8trs). 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 the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form, PDB code: 8trs:

Sodium binding site 1 out of 1 in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Trigonal Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Na404 b:75.1 occ:1.00 O A:HOH478 3.8 62.7 1.0 OE2 D:GLU267 3.8 50.6 1.0 CG2 D:VAL269 4.3 50.9 1.0 O D:HOH524 4.3 57.9 1.0 O D:HOH535 4.3 66.8 1.0 O D:HOH507 4.3 54.5 1.0 CD D:GLU267 4.4 49.9 1.0 OE1 D:GLU267 4.7 47.4 1.0 NE2 D:GLN274 4.7 67.8 1.0

H.A.Bruce, A.U.Singer, E.V.Filippova, L.L.Blazer, J.J.Adams, L.Enderle, M.Ben-David, E.H.Radley, D.Y.L.Mao, V.Pau, S.Orlicky, F.Sicheri, I.Kourinov, S.Atwell, A.A.Kossiakoff, S.S.Sidhu. Engineered Antigen-Binding Fragments For Enhanced Crystallization of Antibody:Antigen Complexes. Protein Sci. E4824 2023.
ISSN: ESSN 1469-896X
PubMed: 37945533
DOI: 10.1002/PRO.4824