Chlorine 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:

Sodium

(Na)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Clathrin N-Terminal Domain in Complex with A Hurp Phospho-Peptide, PDB code: 7zx4:

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl403 b:20.7 occ:1.00 ND2 B:ASN92 3.2 12.7 1.0 ND2 A:ASN92 3.2 15.9 1.0 CB B:ASN92 3.7 15.2 1.0 CG A:MET99 3.7 24.9 1.0 CG B:MET99 3.7 22.1 1.0 CB A:ASN92 3.7 18.1 1.0 CE B:MET99 3.7 27.8 1.0 CE A:MET99 3.8 25.4 1.0 CG B:ASN92 3.9 14.8 1.0 CG A:ASN92 4.0 16.8 1.0 CG2 A:VAL79 4.1 17.7 1.0 CG2 B:VAL79 4.1 19.7 1.0 CE B:MET95 4.2 26.9 1.0 CE A:MET95 4.3 24.8 1.0 CB B:MET99 4.3 21.8 1.0 CB A:MET99 4.4 24.3 1.0 SD B:MET99 4.4 26.4 1.0 SD A:MET99 4.4 23.7 1.0 CA B:ASN92 4.7 16.1 1.0 CA A:ASN92 4.8 19.0 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.