› 1q6h

X-ray diffraction
1.97Å resolution

Crystal structure of a truncated form of FkpA from Escherichia coli

Released:
DOI: 10.2210/pdb1q6h/pdb
PDB entry 1q6h coloured by chain, front view.
PDB entry 1q6h coloured by chain, side view.
PDB entry 1q6h coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.
Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA
J Mol Biol 335 595-608 (2004)
PMID: 14672666

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155308 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FKBP-type peptidyl-prolyl cis-trans isomerase FkpA Chains: A, B
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 24.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P45523 (Residues: 26-249; Coverage: 91%)
Gene names: JW3309, b3347, fkpA, yzzS
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 37.03Å b: 85.23Å c: 160.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.229
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Recombinant protein folding and misfolding in Escherichia coli.
Baneyx et al. (2004)
19 more

3 mentions without citation

Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?
McMorran et al. (2014)
2 more