› 1iga

X-ray solution scattering

MODEL OF HUMAN IGA1 DETERMINED BY SOLUTION SCATTERING CURVE-FITTING AND HOMOLOGY MODELLING

Released:
DOI: 10.2210/pdb1iga/pdb
PDB entry 1iga coloured by chain, front view.
PDB entry 1iga coloured by chain, side view.
PDB entry 1iga coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling.
Boehm MK, Woof JM, Kerr MA, Perkins SJ
J Mol Biol 286 1421-47 (1999)
PMID: 10064707

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208686 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Immunoglobulin heavy constant alpha 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 475 amino acids
Theoretical weight: 51.07 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01876 (Residues: 1-333; Coverage: 84%)
Gene name: IGHA1
Sequence domains:
IGA1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 214 amino acids
Theoretical weight: 23.22 KDa
Source organism: Homo sapiens

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Quick links

Citations

30 review citations

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

14 mentions without citation

IgA: Structure, Function, and Developability.
de Sousa-Pereira et al. (2019)
13 more