› 1fkr

Solution NMR

SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN

Released:
DOI: 10.2210/pdb1fkr/pdb
PDB entry 1fkr coloured by chain, ensemble of 20 models, front view.
PDB entry 1fkr coloured by chain, ensemble of 20 models, side view.
PDB entry 1fkr coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin.
Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL
Science 252 836-9 (1991)
PMID: 1709301

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-158812 (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: 11.84 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
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
Expression system: Not provided

Quick links

Citations

29 review citations

Protein folding in the cell.
Gething et al. (1992)
28 more

4 mentions without citation

Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles.
Chaudhury et al. (2008)
3 more