6x00

X-ray diffraction
1.55Å resolution

Structure of DbNA(11) peptides bound to H-2Db MHC-I

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-135283 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
H-2 class I histocompatibility antigen, D-B alpha chain Chain: A
Molecule details ›
Chain: A
Length: 281 amino acids
Theoretical weight: 32.6 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01899 (Residues: 25-304; Coverage: 83%)
Gene name: H2-D1
Sequence domains:
Beta-2-microglobulin Chain: B
Molecule details ›
Chain: B
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Neuraminidase Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 999 Da
Source organism: Influenza A virus
Expression system: Not provided
UniProt:
  • Canonical: P03468 (Residues: 181-191; Coverage: 2%)
Gene name: NA

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 69.01Å b: 44.751Å c: 71.657Å
α: 90° β: 98.45° γ: 90°
R-values:
R R work R free
0.186 0.184 0.215
Expression systems:
  • Escherichia coli
  • Not provided