2bh3

X-ray diffraction
2.4Å resolution

Zn substituted E. coli Aminopeptidase P in complex with product

Released:

Function and Biology Details

Reaction catalysed:
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.74 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15034 (Residues: 2-441; Coverage: 100%)
Gene names: JW2876, b2908, pepP
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: I4122
Unit cell:
a: 138.012Å b: 138.012Å c: 230.734Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.201
Expression system: Escherichia coli