3il0

X-ray diffraction
2.2Å resolution

The crystal structure of the aminopeptidase P,XAA-pro aminopeptidase from Streptococcus thermophilus

Released:
Entry authors: Zhang R, Hatzos C, Cobb G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-177581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase P XAA-pro aminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.21 KDa
Source organism: Streptococcus thermophilus LMG 18311
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5M2R3 (Residues: 1-128; Coverage: 36%)
Gene names: pepP, stu1742
Sequence domains: Creatinase/Prolidase N-terminal domain
Structure domains: Creatinase/prolidase N-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 43.303Å b: 80.396Å c: 100.858Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.237
Expression system: Escherichia coli BL21