Chlorine in PDB 6vfu: Crystal Structure of Human Protocadherin 19 EC1-EC4

The structure of Crystal Structure of Human Protocadherin 19 EC1-EC4, PDB code: 6vfu was solved by O.J.Harrison, J.Brasch, L.Shapiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 3.50
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.971, 108.971, 309.663, 90.00, 90.00, 120.00
R / Rfree (%)	26.5 / 29.2

The structure of Crystal Structure of Human Protocadherin 19 EC1-EC4 also contains other interesting chemical elements:

Nickel	(Ni)	2 atoms
Calcium	(Ca)	27 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Protocadherin 19 EC1-EC4 (pdb code 6vfu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Human Protocadherin 19 EC1-EC4, PDB code: 6vfu:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Human Protocadherin 19 EC1-EC4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Protocadherin 19 EC1-EC4 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl516 b:0.1 occ:1.00 HA3 C:GLY247 3.7 0.7 1.0 HG2 C:GLU246 3.8 0.7 1.0 H C:THR248 4.0 1.0 1.0 O C:GLU246 4.3 0.8 1.0 HG23 C:THR248 4.5 0.3 1.0 CA C:GLY247 4.6 0.6 1.0 CG C:GLU246 4.7 0.6 1.0 N C:THR248 4.7 0.3 1.0 OG1 C:THR248 4.7 0.7 1.0 C C:GLU246 4.8 0.3 1.0 HB3 C:GLU246 4.8 0.7 1.0 HG1 C:THR248 4.9 0.6 1.0 H C:ASN249 5.0 0.8 1.0 N C:GLY247 5.0 0.6 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Human Protocadherin 19 EC1-EC4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Protocadherin 19 EC1-EC4 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl517 b:0.1 occ:1.00 O C:PHE153 2.8 0.2 1.0 O C:ASN150 2.9 1.0 1.0 HG3 C:GLU172 3.0 0.6 1.0 HA2 C:GLY154 3.5 0.4 1.0 C C:PHE153 3.7 0.9 1.0 HA3 C:GLY154 3.8 0.4 1.0 HA C:GLU151 3.9 0.4 1.0 OD1 C:ASN150 3.9 0.5 1.0 CA C:GLY154 4.0 0.8 1.0 CG C:GLU172 4.0 0.3 1.0 C C:ASN150 4.0 0.0 1.0 N C:GLY154 4.2 0.7 1.0 H C:ASN150 4.2 0.4 1.0 HG2 C:GLU172 4.4 0.6 1.0 O C:GLU151 4.5 0.3 1.0 CA C:GLU151 4.5 0.2 1.0 HD11 C:LEU147 4.5 0.3 1.0 C C:GLU151 4.5 0.0 1.0 H C:PHE153 4.5 0.4 1.0 HB2 C:GLU172 4.5 0.4 1.0 CD C:GLU172 4.6 0.8 1.0 N C:GLU151 4.7 0.8 1.0 CB C:GLU172 4.7 0.7 1.0 N C:PHE153 4.7 0.7 1.0 HB3 C:GLU172 4.7 0.4 1.0 CA C:PHE153 4.8 0.9 1.0 H C:GLY154 4.9 0.2 1.0 N C:ASN150 4.9 0.5 1.0 CG C:ASN150 5.0 0.5 1.0 OE1 C:GLU172 5.0 0.8 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Human Protocadherin 19 EC1-EC4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Protocadherin 19 EC1-EC4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl514 b:0.1 occ:1.00 HG12 A:VAL17 3.9 0.2 1.0 HG11 A:VAL17 4.2 0.2 1.0 HA A:ALA19 4.4 0.0 1.0 CG1 A:VAL17 4.5 0.9 1.0 HB A:VAL17 4.7 0.9 1.0 O A:VAL17 4.7 0.5 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Human Protocadherin 19 EC1-EC4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Human Protocadherin 19 EC1-EC4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl515 b:0.1 occ:1.00 OE1 A:GLN269 3.0 0.9 1.0 CD A:GLN269 4.2 0.3 1.0 HG1 A:THR280 4.2 0.5 1.0 HB2 A:GLN269 4.2 0.1 1.0 HG21 A:THR280 4.4 0.3 1.0 HB3 A:GLN269 4.5 0.1 1.0 CB A:GLN269 4.8 0.7 1.0 OG1 A:THR280 4.9 0.4 1.0 HE22 A:GLN269 4.9 0.3 1.0

O.J.Harrison, J.Brasch, P.S.Katsamba, G.Ahlsen, A.J.Noble, H.Dan, R.V.Sampogna, C.S.Potter, B.Carragher, B.Honig, L.Shapiro. Family-Wide Structural and Biophysical Analysis of Binding Interactions Among Non-Clustered Delta-Protocadherins. Cell Rep V. 30 2655 2020.
ISSN: ESSN 2211-1247
PubMed: 32101743
DOI: 10.1016/J.CELREP.2020.02.003