PDBe 1yat

X-ray diffraction
2.5Å resolution

IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FK506-binding protein 1 Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 12.04 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P20081 (Residues: 2-114; Coverage: 99%)
Gene names: FKB1, FPR1, N1213, N1845, RBP1, YNL135C
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P63
Unit cell:
a: 79.681Å b: 79.681Å c: 54.063Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 not available not available
Expression system: Not provided