› 1yr2

X-ray diffraction
1.8Å resolution

Structural and Mechanistic Analysis of Two Prolyl Endopeptidases: Role of Inter-Domain Dynamics in Catalysis and Specificity

Released:
DOI: 10.2210/pdb1yr2/pdb
PDB entry 1yr2 coloured by chain, front view.
PDB entry 1yr2 coloured by chain, side view.
PDB entry 1yr2 coloured by chain, top view.
Source organism: Novosphingobium capsulatum
Primary publication:
Structural and mechanistic analysis of two prolyl endopeptidases: role of interdomain dynamics in catalysis and specificity.
Shan L, Mathews II, Khosla C
Proc Natl Acad Sci U S A 102 3599-604 (2005)
PMID: 15738423

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195688 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
prolyl oligopeptidase Chain: A
Molecule details ›
Chain: A
Length: 741 amino acids
Theoretical weight: 80.66 KDa
Source organism: Novosphingobium capsulatum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9ZNM8 (Residues: 1-723; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 53.341Å b: 91.224Å c: 79.787Å
α: 90° β: 91° γ: 90°
R-values:
R R work R free
0.162 0.161 0.186
Expression system: Escherichia coli BL21

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Citations

12 review citations

Recent advances in coeliac disease.
van Heel et al. (2006)
11 more

11 mentions without citation

The expanding diversity of serine hydrolases.
Botos et al. (2007)
10 more