› 1h3w

X-ray diffraction
2.85Å resolution

Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

Released:
DOI: 10.2210/pdb1h3w/pdb
PDB entry 1h3w coloured by chain, front view.
PDB entry 1h3w coloured by chain, side view.
PDB entry 1h3w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity.
Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P
J Mol Biol 325 979-89 (2003)
PMID: 12527303

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134849 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Immunoglobulin heavy constant gamma 1 Chain: M
Molecule details ›
Chain: M
Length: 223 amino acids
Theoretical weight: 25.13 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01857 (Residues: 108-328; Coverage: 55%)
Gene name: IGHG1
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, FUC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 49.55Å b: 149.25Å c: 75.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.279 0.279 0.32

Quick links

Citations

111 review citations

The impact of glycosylation on the biological function and structure of human immunoglobulins.
Arnold et al. (2007)
110 more

9 mentions without citation

Function and 3D structure of the N-glycans on glycoproteins.
Nagae et al. (2012)
8 more