5wbh

X-ray diffraction
1.75Å resolution

Structure of the FRB domain of mTOR bound to a substrate recruitment peptide of S6K1

Released:
Source organism: Homo sapiens

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

Assemblies composition:
monomeric
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-149962 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase mTOR Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 102 amino acids
Theoretical weight: 12.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42345 (Residues: 2018-2114; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain
Ribosomal protein S6 kinase beta-1 Chain: W
Molecule details ›
Chain: W
Length: 26 amino acids
Theoretical weight: 3.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23443 (Residues: 412-437; Coverage: 5%)
Gene names: RPS6KB1, STK14A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Unit cell:
a: 60.613Å b: 80.944Å c: 134.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.21
Expression system: Escherichia coli BL21(DE3)