› 5w5m

X-ray diffraction
1.9Å resolution

Crystal structure of human IgG4-Sigma1 Fc fragment

Released:
DOI: 10.2210/pdb5w5m/pdb
PDB entry 5w5m coloured by chain, front view.
PDB entry 5w5m coloured by chain, side view.
PDB entry 5w5m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional, Biophysical, and Structural Characterization of Human IgG1 and IgG4 Fc Variants with Ablated Immune Functionality.
Tam SH, McCarthy SG, Armstrong AA, Somani S, Wu SJ, Liu X, Gervais A, Ernst R, Saro D, Decker R, Luo J, Gilliland GL, Chiu ML, Scallon BJ
OpenAccess logo Antibodies (Basel) 6 (2017)
PMID: 31548527

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Immunoglobulin heavy constant gamma 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 25.03 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P01861 (Residues: 106-325; Coverage: 56%)
  • Best match: P01861-1 (Residues: 106-327)
Gene name: IGHG4
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUC
Carbohydrate polymer
2 bound ligands:
Ligand GOL 2 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 74.74Å b: 78.39Å c: 97.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.225
Expression system: Homo sapiens

Quick links

Citations

6 review citations

Conceptual Approaches to Modulating Antibody Effector Functions and Circulation Half-Life.
Saunders KO. (2019)
5 more

3 mentions without citation

Structure Based Prediction of Asparagine Deamidation Propensity in Monoclonal Antibodies.
Yan et al. (2018)
2 more