› 5kaq

X-ray diffraction
3.51Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-207825 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Hemagglutinin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 512 amino acids
Theoretical weight: 57.33 KDa
Source organism: Influenza A virus (A/Hong Kong/1-4-MA21-1/1968(H3N2))
Expression system: Homo sapiens
UniProt:
  • Canonical: E1AFM4 (Residues: 17-521; Coverage: 89%)
Gene name: HA
Sequence domains: Haemagglutinin
Structure domains: Hemagglutinin (Ha1 Chain); Chain: A; domain 1
ANTIBODY 31.A.83 FAB HEAVY CHAIN Chains: F, H, Q
Molecule details ›
Chains: F, H, Q
Length: 236 amino acids
Theoretical weight: 25.11 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
ANTIBODY 31.A.83 FAB LIGHT CHAIN Chains: G, L, R
Molecule details ›
Chains: G, L, R
Length: 214 amino acids
Theoretical weight: 23.51 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand NAG 18 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 279.435Å b: 154.283Å c: 157.937Å
α: 90° β: 116.86° γ: 90°
R-values:
R R work R free
0.272 0.27 0.313
Expression system: Homo sapiens

Quick links

Citations

54 review citations

Tfh cells and HIV bnAbs, an immunodominance model of the HIV neutralizing antibody generation problem.
Havenar-Daughton et al. (2017)
53 more

7 mentions without citation

Insights into the Structural Basis of Antibody Affinity Maturation from Next-Generation Sequencing.
Mishra et al. (2018)
6 more