4dt4

X-ray diffraction
1.35Å resolution

Crystal structure of the PPIase-chaperone SlpA with the chaperone binding site occupied by the linker of the purification tag

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.27 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEM0 (Residues: 1-149; Coverage: 100%)
Gene names: JW0026, b0028, fkpB, slpA, yaaD
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 40.12Å b: 29.23Å c: 60.69Å
α: 90° β: 93.2° γ: 90°
R-values:
R R work R free
0.161 0.16 0.201
Expression system: Escherichia coli