Chlorine in PDB 3o4d: Crystal Structure of Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure

The structure of Crystal Structure of Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure, PDB code: 3o4d was solved by J.Lee, M.Blaber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.39 / 1.65
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	50.372, 53.151, 84.780, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 22.6

The binding sites of Chlorine atom in the Crystal Structure of Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure (pdb code 3o4d). 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 Crystal Structure of Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure, PDB code: 3o4d:

Chlorine binding site 1 out of 1 in the Crystal Structure of Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure


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 Symfoil-4P: De Novo Designed Beta-Trefoil Architecture with Symmetric Primary Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl143 b:47.8 occ:1.00 N A:ASP114 3.3 28.0 1.0 CG A:ASP114 3.3 30.1 1.0 CD A:PRO113 3.3 25.2 1.0 OD2 A:ASP114 3.6 26.3 1.0 OD1 A:ASP114 3.6 29.2 1.0 CB A:ASP114 3.6 25.9 1.0 N A:PRO113 3.7 23.4 1.0 CB A:ASN112 3.7 22.2 1.0 CG A:PRO113 4.0 31.4 1.0 CB A:PRO113 4.0 27.9 1.0 CA A:ASP114 4.0 25.5 1.0 C A:PRO113 4.1 22.1 1.0 CA A:PRO113 4.2 29.3 1.0 C A:ASN112 4.2 22.0 1.0 CA A:ASN112 4.5 19.8 1.0 O A:HOH185 4.7 36.4 1.0 CG A:ASN112 4.7 19.4 1.0 O A:HOH236 4.9 35.4 1.0

J.Lee, M.Blaber. Experimental Support For the Evolution of Symmetric Protein Architecture From A Simple Peptide Motif. Proc.Natl.Acad.Sci.Usa V. 108 126 2011.
ISSN: ISSN 0027-8424
PubMed: 21173271
DOI: 10.1073/PNAS.1015032108