› 6r9z

Solution NMR

3D NMR solution structure of ligand peptide (Ac)EVNPPVP of Pro-Pro endopeptidase-1

Released:
DOI: 10.2210/pdb6r9z/pdb
PDB entry 6r9z coloured by chain, ensemble of 20 models, front view.
PDB entry 6r9z coloured by chain, ensemble of 20 models, side view.
PDB entry 6r9z coloured by chain, ensemble of 20 models, top view.
Source organism: Clostridioides difficile
Primary publication:
Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1.
Pichlo C, Juetten L, Wojtalla F, Schacherl M, Diaz D, Baumann U
J Biol Chem 294 11525-11535 (2019)
PMID: 31182482

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ACE-GLU-VAL-ASN-PRO-PRO-VAL-PRO-NH2 Chain: A
Molecule details ›
Chain: A
Length: 9 amino acids
Theoretical weight: 775 Da
Source organism: Clostridioides difficile
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 44%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

2 review citations

Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.
van Leeuwen et al. (2021)
1 more

2 mentions without citation

Enhancing subtilisin thermostability through a modified normalized B-factor analysis and loop-grafting strategy.
Tang et al. (2019)
1 more