2bhd

X-ray diffraction
2.5Å resolution

Mg 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:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-537809 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
VALINE-PROLINE-LEUCINE TRIPEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 327 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: I4122
Unit cell:
a: 138.569Å b: 138.569Å c: 230.962Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.204
Expression systems:
  • Escherichia coli
  • Not provided