› 3n2z

X-ray diffraction
2.79Å resolution

The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution

Released:
DOI: 10.2210/pdb3n2z/pdb
PDB entry 3n2z coloured by chain, front view.
PDB entry 3n2z coloured by chain, side view.
PDB entry 3n2z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
Soisson SM, Patel SB, Abeywickrema PD, Byrne NJ, Diehl RE, Hall DL, Ford RE, Reid JC, Rickert KW, Shipman JM, Sharma S, Lumb KJ
BMC Struct Biol 10 16 (2010)
PMID: 20540760

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154873 (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
Carbohydrate polymer
2 bound ligands:
Ligand NAG 4 x NAG
Ligand SO4 1 x SO4
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

Quick links

Citations

5 review citations

The metabolic serine hydrolases and their functions in mammalian physiology and disease.
Long et al. (2011)
4 more

11 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
10 more