› 1h3v

X-ray diffraction
3.1Å resolution

CRYSTAL STRUCTURE OF THE HUMAN IGG1 FC-FRAGMENT,GLYCOFORM (G2F)2,SG P212121

Released:
DOI: 10.2210/pdb1h3v/pdb
PDB entry 1h3v coloured by chain, front view.
PDB entry 1h3v coloured by chain, side view.
PDB entry 1h3v 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 (3 distinct):
Immunoglobulin heavy constant gamma 1 Chains: A, B
Molecule details ›
Chains: A, B
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, MAN, GAL, FUL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUL
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 49.47Å b: 80.85Å c: 141.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.314

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

13 mentions without citation

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