4hom

X-ray diffraction
1.9Å resolution

Crystal structure of porcine aminopeptidase-N complexed with substance P

Released:
Source organisms:
Primary publication:
Structural basis for multifunctional roles of mammalian aminopeptidase N.
Proc Natl Acad Sci U S A 109 17966-71 (2012)
PMID: 23071329

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-147241 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 908 amino acids
Theoretical weight: 103.52 KDa
Source organism: Sus scrofa
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P15145 (Residues: 63-963; Coverage: 94%)
Gene name: ANPEP
Sequence domains:
Structure domains:
Substance P Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20366 (Residues: 58-68; Coverage: 10%)
Gene names: NKA, NKNA, TAC1, TAC2
Sequence domains: Tachykinin family

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 261.573Å b: 62.598Å c: 81.553Å
α: 90° β: 100.27° γ: 90°
R-values:
R R work R free
0.15 0.147 0.201
Expression systems:
  • Spodoptera frugiperda
  • Not provided