› 1lns

X-ray diffraction
2.2Å resolution

Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

Released:
DOI: 10.2210/pdb1lns/pdb
PDB entry 1lns coloured by chain, front view.
PDB entry 1lns coloured by chain, side view.
PDB entry 1lns coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis.
Rigolet P, Mechin I, Delage MM, Chich JF
Structure 10 1383-94 (2002)
PMID: 12377124

Function and Biology Details

Reaction catalysed: 
Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidyl-peptidase Chain: A
Molecule details ›
Chain: A
Length: 763 amino acids
Theoretical weight: 87.8 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: P22346 (Residues: 1-763; Coverage: 100%)
Gene name: pepX
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21212
Unit cell:
a: 92.5Å b: 102.5Å c: 101.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.223
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome.
Rawlings et al. (2008)
9 more

3 mentions without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)
2 more