2iw2

X-ray diffraction
1.82Å resolution

Crystal structure of human Prolidase

Released:
Source organism: Homo sapiens
Entry authors: Mueller U, Niesen FH, Roske Y, Goetz F, Behlke J, Buessow K, Heinemann U

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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2221
Unit cell:
a: 103.579Å b: 108.518Å c: 211.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.192
Expression system: Escherichia coli