Chlorine in PDB 5yc5: Crystal Structure of Human Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia

The structure of Crystal Structure of Human Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia, PDB code: 5yc5 was solved by J.M.M.Caaveiro, H.Tamura, K.Tsumoto, M.Kiyoshi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.90 / 2.71
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.790, 101.420, 122.600, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 27.3

The binding sites of Chlorine atom in the Crystal Structure of Human Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia (pdb code 5yc5). 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 Human Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia, PDB code: 5yc5:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia


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 Igg-Fc in Complex with Aglycan and Optimized Fc Gamma Receptor Iiia within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1012 b:78.5 occ:1.00 OE2 A:GLU333 3.2 70.8 1.0 NZ A:LYS322 3.5 65.8 1.0 NZ A:LYS320 3.6 64.6 1.0 CD A:GLU333 4.2 66.2 1.0 OH A:TYR278 4.2 63.9 1.0 CZ A:TYR278 4.3 60.5 1.0 OE1 A:GLU333 4.5 65.8 1.0 CE2 A:TYR278 4.6 59.3 1.0 CE A:LYS322 4.6 63.6 1.0 CE A:LYS320 4.8 61.8 1.0 CE1 A:TYR278 4.8 59.8 1.0 CD A:LYS322 4.8 60.0 1.0

M.Kiyoshi, J.M.M.Caaveiro, M.Tada, H.Tamura, T.Tanaka, Y.Terao, K.Morante, A.Harazono, N.Hashii, H.Shibata, D.Kuroda, S.Nagatoishi, S.Oe, T.Ide, K.Tsumoto, A.Ishii-Watabe. Assessing the Heterogeneity of the Fc-Glycan of A Therapeutic Antibody Using An Engineered Fc Gamma Receptor Iiia-Immobilized Column. Sci Rep V. 8 3955 2018.
ISSN: ESSN 2045-2322
PubMed: 29500371
DOI: 10.1038/S41598-018-22199-8