Structure analysis

The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution

X-ray diffraction
2.79Å resolution
Source organism: Homo sapiens
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: 37136.74 Å2
Buried surface area: 6947.95 Å2
Dissociation area: 2,046.35 Å2
Dissociation energy (ΔGdiss): 10.77 kcal/mol
Dissociation entropy (TΔSdiss): 14.71 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-154873

Macromolecules

Chain: B
Length: 446 amino acids
Theoretical weight: 50.57 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P42785 (Residues: 46-491; Coverage: 94%)
Gene names: PCP, PRCP
Pfam: Serine carboxypeptidase S28
InterPro:
CATH:

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