PDBe 1azw

X-ray diffraction
2.7Å resolution

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

Released:

Function and Biology Details

Reaction catalysed:
Release of N-terminal proline from a peptide. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline iminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 313 amino acids
Theoretical weight: 35.52 KDa
Source organism: Xanthomonas citri
Expression system: Escherichia coli
UniProt:
  • Canonical: P52279 (Residues: 1-313; Coverage: 100%)
Gene names: pip, xap
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C222
Unit cell:
a: 147.2Å b: 167.8Å c: 85.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.253
Expression system: Escherichia coli