PDBe 4fap

X-ray diffraction
2.8Å resolution

ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP

Released:
Source organism: Homo sapiens
Primary publication:
Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 55 736-44 (1999)
PMID: 10089303

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Serine/threonine-protein kinase mTOR Chain: B
Molecule details ›
Chain: B
Length: 94 amino acids
Theoretical weight: 11.33 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P42345 (Residues: 2019-2112; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Structure domains: FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 45.4Å b: 52.1Å c: 102.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.266
Expression system: Escherichia coli