PDBe 2dg3

X-ray diffraction
1.7Å resolution

Wildtype FK506-binding protein complexed with Rapamycin

Released:
Source organism: Homo sapiens
Primary publication:
Energetic and structural analysis of the role of tryptophan 59 in FKBP12.
Biochemistry 42 2364-72 (2003)
PMID: 12600203

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: Escherichia coli BL21
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-13
Spacegroup: P212121
Unit cell:
a: 44.604Å b: 48.841Å c: 53.966Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.228
Expression system: Escherichia coli BL21