› 2rse

Solution NMR

NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS

Released:
DOI: 10.2210/pdb2rse/pdb
PDB entry 2rse coloured by chain, ensemble of 20 models, front view.
PDB entry 2rse coloured by chain, ensemble of 20 models, side view.
PDB entry 2rse coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.
Kobashigawa Y, Saio T, Ushio M, Sekiguchi M, Yokochi M, Ogura K, Inagaki F
J Biomol NMR 53 53-63 (2012)
PMID: 22487935

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154618 (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
Expression system: Escherichia coli
UniProt:
  • Canonical: P42345 (Residues: 2019-2112; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Sequence domains: FKBP12-rapamycin binding domain
Structure domains: FKBP12-rapamycin binding domain

Ligands and Environments

1 bound ligand:
Ligand TB 2 x TB
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 53%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

NMR approaches for structural analysis of multidomain proteins and complexes in solution.
Göbl et al. (2014)
4 more

3 mentions without citation

Targeting protein-protein interaction interfaces in COVID-19 drug discovery.
Chang et al. (2021)
2 more