2okn

X-ray diffraction
2.45Å resolution

Crystal Strcture of Human Prolidase

Released:
Source organism: Homo sapiens
Entry authors: Mueller U, Niesen FH, Roske Y, Goetz F, Behlke J, Buessow K, Heinemann U, Protein Structure Factory (PSF)

Function and Biology Details

Reaction catalysed:
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 494 amino acids
Theoretical weight: 54.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P12955 (Residues: 2-493; Coverage: 100%)
Gene names: PEPD, PRD
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 103.89Å b: 108.96Å c: 212.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.231
Expression system: Escherichia coli