› 4lay

X-ray diffraction
1.7Å resolution

Crystal Structure Analysis of FKBP52, Complex with I63

Released:
DOI: 10.2210/pdb4lay/pdb
PDB entry 4lay coloured by chain, front view.
PDB entry 4lay coloured by chain, side view.
PDB entry 4lay coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the free and ligand-bound FK1-FK2 domain segment of FKBP52 reveal a flexible inter-domain hinge.
Bracher A, Kozany C, Hähle A, Wild P, Zacharias M, Hausch F
J Mol Biol 425 4134-44 (2013)
PMID: 23933011

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-169761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02790 (Residues: 1-260; Coverage: 57%)
Gene names: FKBP4, FKBP52
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand I63 1 x I63
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 47.592Å b: 42.351Å c: 76.811Å
α: 90° β: 105.75° γ: 90°
R-values:
R R work R free
0.17 0.168 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

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

4 mentions without citation

Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.
Dunyak et al. (2016)
3 more