PDBe 3o5i

X-ray diffraction
1.8Å resolution

Fk1 domain of FKBP51, crystal form II

Released:
Source organism: Homo sapiens
Primary publication:
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.
Acta Crystallogr. D Biol. Crystallogr. 67 549-59 (2011)
PMID: 21636895

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 128 amino acids
Theoretical weight: 14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 48.353Å b: 48.353Å c: 180.478Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.246
Expression system: Escherichia coli