› 4c7w

X-ray diffraction
2.5Å resolution

Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase in complex with 4-O-acetylated sialic acid

Released:
DOI: 10.2210/pdb4c7w/pdb
PDB entry 4c7w coloured by chain, front view.
PDB entry 4c7w coloured by chain, side view.
PDB entry 4c7w coloured by chain, top view.
Source organism: Murine hepatitis virus
Primary publication:
The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture.
Langereis MA, Zeng Q, Heesters BA, Huizinga EG, de Groot RJ, de Groot RJ
PLoS Pathog 8 e1002492 (2012)
PMID: 22291594

Function and Biology Details

Reaction catalysed: 
N-acetyl-O-acetylneuraminate + H(2)O = N-acetylneuraminate + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Hemagglutinin-esterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 43.5 KDa
Source organism: Murine hepatitis virus
Expression system: Homo sapiens
UniProt:
  • Canonical: P31614 (Residues: 25-403; Coverage: 91%)
Gene names: 2b, HE
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
4 bound ligands:
Ligand SIO 2 x SIO
Ligand K 2 x K
Ligand NAG 4 x NAG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 91.566Å b: 106.59Å c: 135.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.214 0.249
Expression system: Homo sapiens

Quick links

Citations

10 review citations

Biological roles of glycans.
Varki A. (2017)
9 more

3 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
2 more