PDBe 3o5k

X-ray diffraction
2.7Å resolution

Fk1 domain of FKBP51, crystal form VIII

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:
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, C, D
Molecule details ›
Chains: A, B, C, D
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

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: 69.802Å b: 48.43Å c: 76.317Å
α: 90° β: 114.5° γ: 90°
R-values:
R R work R free
0.227 0.224 0.283
Expression system: Escherichia coli