1fxk

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only hexamer (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
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:

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