› 1fkl

X-ray diffraction
1.7Å resolution

ATOMIC STRUCTURE OF FKBP12-RAPAYMYCIN, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX

Released:
DOI: 10.2210/pdb1fkl/pdb
PDB entry 1fkl coloured by chain, front view.
PDB entry 1fkl coloured by chain, side view.
PDB entry 1fkl coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin.
Wilson KP, Yamashita MM, Sintchak MD, Rotstein SH, Murcko MA, Boger J, Thomson JA, Fitzgibbon MJ, Black JR, Navia MA
Acta Crystallogr D Biol Crystallogr 51 511-21 (1995)
PMID: 15299838

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-538875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.79 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P18203 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 48.9Å b: 49.5Å c: 55.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available

Quick links

Citations

5 review citations

Immunophilins: switched on protein binding domains?
Ivery MT. (2000)
4 more

7 mentions without citation

Interactions of FK506 and Rapamycin With FK506 Binding Protein 12 in Opportunistic Human Fungal Pathogens.
Vellanki et al. (2020)
6 more