PDBe 6atk

X-ray diffraction
3.5Å resolution

Crystal structure of the human coronavirus 229E spike protein receptor binding domain in complex with human aminopeptidase N

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aminopeptidase N Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 905 amino acids
Theoretical weight: 103.46 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P15144 (Residues: 66-967; Coverage: 93%)
Gene names: ANPEP, APN, CD13, PEPN
Sequence domains:
Spike glycoprotein Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 146 amino acids
Theoretical weight: 15.87 KDa
Source organism: Human coronavirus 229E
Expression system: Homo sapiens
UniProt:
  • Canonical: P15423 (Residues: 293-435; Coverage: 12%)
Gene names: 2, S

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P3121
Unit cell:
a: 153.82Å b: 153.82Å c: 322.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.244 0.267
Expression system: Homo sapiens