X-ray diffraction
2.3Å resolution

Crystal Structure of E. coli PepN (Aminopeptidase N)in complex with Bestatin

Source organism: Escherichia coli K-12
Primary publication:
Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site.
Proc. Natl. Acad. Sci. U.S.A. 103 13339-44 (2006)
PMID: 16938892

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 891 amino acids
Theoretical weight: 101.44 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P04825 (Residues: 1-870; Coverage: 100%)
Gene names: JW0915, b0932, pepN
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P3121
Unit cell:
a: 120.67Å b: 120.67Å c: 170.84Å
α: 90° β: 90° γ: 120°
R R work R free
0.181 0.154 0.202
Expression system: Escherichia coli BL21(DE3)