› 2kgj

Solution NMR

Solution structure of parvulin domain of PpiD from E.Coli

Released:
DOI: 10.2210/pdb2kgj/pdb
PDB entry 2kgj coloured by chain, ensemble of 10 models, front view.
PDB entry 2kgj coloured by chain, ensemble of 10 models, side view.
PDB entry 2kgj coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity.
Weininger U, Jakob RP, Kovermann M, Balbach J, Schmid FX
Protein Sci 19 6-18 (2010)
PMID: 19866485

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic chaperone PpiD Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.17 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ADY1 (Residues: 264-357; Coverage: 15%)
Gene names: JW0431, b0441, ppiD, ybaU
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
Chemical shift assignment: 58%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The Bam machine: a molecular cooper.
Ricci et al. (2012)
9 more

2 mentions without citation

The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity.
Weininger et al. (2010)
1 more