X-ray diffraction
2.8Å resolution

Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2


Function and Biology Details

Reaction catalysed:
Angiotensin II + H(2)O = angiotensin-(1-7) + L-phenylalanine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Processed angiotensin-converting enzyme 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 597 amino acids
Theoretical weight: 69.08 KDa
Source organisms: Expression system: Spodoptera frugiperda
  • Canonical: Q56NL1 (Residues: 21-55; Coverage: 4%)
  • Canonical: Q9BYF1 (Residues: 19-20, 56-615; Coverage: 71%)
Gene names: ACE2, UNQ868/PRO1885
Sequence domains: Angiotensin-converting enzyme
Spike protein S1 Chains: E, F
Molecule details ›
Chains: E, F
Length: 179 amino acids
Theoretical weight: 20.42 KDa
  • Canonical: P59594 (Residues: 324-502; Coverage: 14%)
Gene names: 2, S
Sequence domains: Betacoronavirus spike glycoprotein S1, receptor binding
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 80.008Å b: 119.762Å c: 108.801Å
α: 90° β: 96.22° γ: 90°
R R work R free
0.217 0.214 0.279
Expression system: Spodoptera frugiperda