› 1jns

Solution NMR

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

Released:
DOI: 10.2210/pdb1jns/pdb
PDB entry 1jns coloured by chain, ensemble of 18 models, front view.
PDB entry 1jns coloured by chain, ensemble of 18 models, side view.
PDB entry 1jns coloured by chain, ensemble of 18 models, 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:
  • not assigned
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: simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

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

6 mentions without citation

Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.
Heikkinen et al. (2009)
5 more