1c9h

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

Released:
Source organism: Homo sapiens
Primary publication:
Structure of FKBP12.6 in complex with rapamycin.
Acta Crystallogr. D Biol. Crystallogr. 56 266-71 (2000)
PMID: 10713512

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1B Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
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
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 45.696Å b: 49.288Å c: 51.694Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.249
Expression system: Escherichia coli