Chlorine in PDB 5xjf: Crystal Structure of Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of Fc Gamma Receptor Iiia

The structure of Crystal Structure of Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of Fc Gamma Receptor Iiia, PDB code: 5xjf was solved by Y.Sakae, T.Satoh, H.Yagi, S.Yanaka, T.Yamaguchi, Y.Isoda, S.Iida, Y.Okamoto, K.Kato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.300, 77.300, 349.800, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 27

The binding sites of Chlorine atom in the Crystal Structure of Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of Fc Gamma Receptor Iiia (pdb code 5xjf). 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 Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of Fc Gamma Receptor Iiia, PDB code: 5xjf:

Chlorine binding site 1 out of 1 in the Crystal Structure of Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of 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 Fucosylated Igg Fc Y296W Mutant Complexed with Bis-Glycosylated Soluble Form of Fc Gamma Receptor Iiia within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1010 b:82.9 occ:1.00 O A:HOH1137 3.5 62.7 1.0 CD1 A:PHE243 4.1 55.4 1.0 C3 A:NAG1007 4.1 67.8 1.0 N2 A:NAG1007 4.4 64.1 1.0 CD A:PRO244 4.5 62.6 1.0 CE1 A:PHE243 4.7 58.0 1.0 C2 A:NAG1007 4.7 65.6 1.0 O3 A:NAG1007 4.7 65.1 1.0 O4 A:NAG1007 4.8 78.4 1.0 CG A:PRO244 4.9 60.0 1.0 CG A:PHE243 5.0 54.1 1.0 C1 A:NAG1007 5.0 65.3 1.0

Y.Sakae, T.Satoh, H.Yagi, S.Yanaka, T.Yamaguchi, Y.Isoda, S.Iida, Y.Okamoto, K.Kato. Conformational Effects of N-Glycan Core Fucosylation of Immunoglobulin G Fc Region on Its Interaction with Fc Gamma Receptor Iiia. Sci Rep V. 7 13780 2017.
ISSN: ESSN 2045-2322
PubMed: 29062024
DOI: 10.1038/S41598-017-13845-8