PDBe 2hpo

X-ray diffraction
1.65Å resolution

Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site

Released:
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
Macromolecule:
Aminopeptidase N Chain: A

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P3121
Unit cell:
a: 120.438Å b: 120.438Å c: 170.561Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.157 0.181
Expression system: Escherichia coli