PDBe 1fap

X-ray diffraction
2.7Å resolution

THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP

Released:

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein. 
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase mTOR Chain: B
Molecule details ›
Chain: B
Length: 95 amino acids
Theoretical weight: 11.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42345 (Residues: 2018-2112; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Structure domains: FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)
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
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.63Å b: 52.14Å c: 102.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.299
Expression system: Escherichia coli