PDBe 1aue

X-ray diffraction
2.33Å resolution

FKBP-RAPAMYCIN BINDING DOMAIN (FRB) OF THE FKBP-RAPAMYCIN ASSOCIATED PROTEIN

Released:
Source organism: Homo sapiens
Primary publication:
Structural Basis for Peptidomimicry by the Effector Element of Rapamycin
J. Am. Chem. Soc. 119 10253-10254 (1997)

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase mTOR Chains: A, B
Molecule details ›
Chains: A, B
Length: 100 amino acids
Theoretical weight: 12.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P42345 (Residues: 2015-2114; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P212121
Unit cell:
a: 29.94Å b: 59.21Å c: 123.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.339
Expression system: Escherichia coli BL21