Sodium in PDB 7zx4: Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide

The structure of Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide, PDB code: 7zx4 was solved by J.Kliche, D.Badgujar, D.Dobritzsch, Y.Ivarsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.20 / 2.08
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.774, 94.242, 88.981, 90, 103.81, 90
R / Rfree (%)	20.6 / 24.9

The structure of Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide (pdb code 7zx4). 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 Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide, PDB code: 7zx4:

Sodium binding site 1 out of 1 in the Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na404 b:55.6 occ:1.00 O A:HOH623 2.7 28.5 1.0 CD1 A:ILE154 3.2 24.9 1.0 CG1 A:VAL262 3.6 19.6 1.0 CB A:VAL262 3.7 19.2 1.0 CA A:VAL262 3.8 18.6 1.0 CD1 A:ILE170 4.0 28.5 1.0 CE2 A:PHE260 4.0 20.7 1.0 O A:VAL262 4.2 22.0 1.0 O A:PRO261 4.5 17.1 1.0 CG1 A:ILE154 4.5 23.3 1.0 C A:VAL262 4.5 18.9 1.0 CG2 A:ILE170 4.6 28.7 1.0 C1 A:GOL402 4.6 43.5 1.0 CG2 A:ILE154 4.6 22.9 1.0 CB A:ILE154 4.7 21.9 1.0 CZ A:PHE260 4.8 23.3 1.0 CD2 A:PHE260 4.9 20.6 1.0 O1 A:GOL402 4.9 45.8 1.0 O A:HOH537 4.9 36.0 1.0 N A:VAL262 5.0 17.8 1.0

J.Kliche, D.H.Garvanska, L.Simonetti, D.Badgujar, D.Ochoa, P.Beltrao, D.Dobritzsch, J.Nilsson, N.Davey, Y.Ivarsson. Large-Scale Identification of Phospho-Modulated Motif-Based Protein-Protein Interactions To Be Published.