› 1jnt

Solution NMR

NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10

Released:
DOI: 10.2210/pdb1jnt/pdb
PDB entry 1jnt coloured by chain, front view.
PDB entry 1jnt coloured by chain, side view.
PDB entry 1jnt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.
Kühlewein A, Voll G, Hernandez Alvarez B, Kessler H, Fischer G, Rahfeld JU, Gemmecker G
Protein Sci 13 2378-87 (2004)
PMID: 15322281

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase C Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 10.12 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9L5 (Residues: 2-93; Coverage: 99%)
Gene names: JW3748, b3775, parVA, ppiC
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: The averaged structure of the ensemble (1JNS) was regularized under experimental constraints
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Prolyl isomerization and its catalysis in protein folding and protein function.
Schmidpeter et al. (2015)
15 other articles

6 mentions without citation

Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.
Ünal et al. (2014)
5 more