5mc2

X-ray diffraction
1.7Å resolution

Crystal Structure of Gly278Asp mutant of Human Prolidase with Mn ions and GlyPro ligand

Released:

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
Macromolecule:
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 484 amino acids
Theoretical weight: 53.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P12955 (Residues: 6-488; 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: 103.842Å b: 108.247Å c: 211.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.141 0.171
Expression system: Escherichia coli BL21