1wy2

X-ray diffraction
1.7Å resolution

Crystal Structure of the Prolidase from Pyrococcus horikoshii OT3

Released:
Source organism: Pyrococcus horikoshii OT3
Entry authors: Mizutani H, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-129783 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 39.46 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58885 (Residues: 1-351; Coverage: 100%)
Gene names: PH1149, pepQ
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 66.697Å b: 105.876Å c: 106.291Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.21
Expression system: Escherichia coli