3n2z

X-ray diffraction
2.79Å resolution

The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysosomal Pro-X carboxypeptidase Chain: B
Molecule details ›
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
Sequence domains: Serine carboxypeptidase S28
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: R32
Unit cell:
a: 181.14Å b: 181.14Å c: 240.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.244
Expression system: Cricetulus griseus