› 1p5q

X-ray diffraction
2.8Å resolution

Crystal Structure of FKBP52 C-terminal Domain

Released:
DOI: 10.2210/pdb1p5q/pdb
PDB entry 1p5q coloured by chain, front view.
PDB entry 1p5q coloured by chain, side view.
PDB entry 1p5q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.
Wu B, Li P, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, Rao Z
Proc Natl Acad Sci U S A 101 8348-53 (2004)
PMID: 15159550

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 domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169763 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 336 amino acids
Theoretical weight: 38.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02790 (Residues: 146-459; Coverage: 68%)
Gene names: FKBP4, FKBP52
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 9 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 114.274Å b: 142.927Å c: 170.897Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.212 0.284
Expression system: Escherichia coli

Quick links

Citations

22 review citations

How corticosteroids control inflammation: Quintiles Prize Lecture 2005.
Barnes PJ. (2006)
21 more

18 mentions without citation

FKBP51 and FKBP52 in signaling and disease.
Storer et al. (2011)
17 more