› 3o5d

X-ray diffraction
4Å resolution

Crystal structure of a fragment of FKBP51 comprising the Fk1 and Fk2 domains

Released:
DOI: 10.2210/pdb3o5d/pdb
PDB entry 3o5d coloured by chain, front view.
PDB entry 3o5d coloured by chain, side view.
PDB entry 3o5d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.
Bracher A, Kozany C, Thost AK, Hausch F
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:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 29.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13451 (Residues: 1-260; Coverage: 57%)
Gene names: AIG6, FKBP5, FKBP51
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I41
Unit cell:
a: 113.73Å b: 113.73Å c: 112.126Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.319 0.317 0.344
Expression system: Escherichia coli

Quick links

Citations

7 review citations

FKBP Ligands-Where We Are and Where to Go?
Kolos et al. (2018)
6 more

3 mentions without citation

Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.
Thapar R. (2015)
2 more