X-ray diffraction
1.8Å resolution

Crystal Structure of Gly448Arg mutant of Human Prolidase with Mn ions and GlyPro ligand


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 482 amino acids
Theoretical weight: 53.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: P12955 (Residues: 6-487; Coverage: 98%)
Gene names: PEPD, PRD
Sequence domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 103.742Å b: 107.737Å c: 210.878Å
α: 90° β: 90° γ: 90°
R R work R free
0.164 0.163 0.192
Expression system: Escherichia coli BL21