› 1fxk

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).

Released:
DOI: 10.2210/pdb1fxk/pdb
PDB entry 1fxk coloured by chain, front view.
PDB entry 1fxk coloured by chain, side view.
PDB entry 1fxk coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.
Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I
Cell 103 621-32 (2000)
PMID: 11106732

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127853 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Prefoldin subunit beta Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 12.73 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26774 (Residues: 5-111; Coverage: 88%)
Gene names: MTH_678, pfdB
Sequence domains: Prefoldin subunit
Structure domains: Helix Hairpins
Prefoldin subunit beta Chain: B
Molecule details ›
Chain: B
Length: 109 amino acids
Theoretical weight: 12.78 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26774 (Residues: 6-114; Coverage: 90%)
Gene names: MTH_678, pfdB
Sequence domains: Prefoldin subunit
Structure domains: Helix Hairpins
Prefoldin subunit alpha Chain: C
Molecule details ›
Chain: C
Length: 133 amino acids
Theoretical weight: 14.38 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O27646 (Residues: 7-136; Coverage: 92%)
Gene names: MTH_1609, pfdA
Sequence domains: Prefoldin subunit
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21212
Unit cell:
a: 72.85Å b: 90.69Å c: 78.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.266
Expression system: Escherichia coli

Quick links

Citations

43 review citations

Translocation of proteins into mitochondria.
Neupert et al. (2007)
42 more

12 mentions without citation

Classification of intrinsically disordered regions and proteins.
van der Lee et al. (2014)
11 more