PDBe 2dqm

X-ray diffraction
1.6Å resolution

Crystal Structure of Aminopeptidase N complexed with bestatin

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 870 amino acids
Theoretical weight: 99.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • 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: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P3121
Unit cell:
a: 120.417Å b: 120.417Å c: 170.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.182 0.194
Expression system: Escherichia coli