Structure analysis

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

X-ray diffraction
2.7Å resolution
Source organism: Xanthomonas citri
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 23796.63 Å2
Buried surface area: 1225.48 Å2
Dissociation area: 612.74 Å2
Dissociation energy (ΔGdiss): -6.57 kcal/mol
Dissociation entropy (TΔSdiss): 13.32 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-156488

Macromolecules

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
Pfam: alpha/beta hydrolase fold
InterPro:
CATH: alpha/beta hydrolase
SCOP: Proline iminopeptidase-like

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