6m4u

X-ray diffraction
2.2Å resolution

Crystal structure of FKBP-FRB T2098L mutant in complex with rapamycin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-154618 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase FKBP1A Chains: A, E
Molecule details ›
Chains: A, E
Length: 110 amino acids
Theoretical weight: 12.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62942 (Residues: 1-108; Coverage: 100%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Serine/threonine-protein kinase mTOR Chains: B, F
Molecule details ›
Chains: B, F
Length: 95 amino acids
Theoretical weight: 11.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42345 (Residues: 2021-2113; Coverage: 4%)
Gene names: FRAP, FRAP1, FRAP2, MTOR, RAFT1, RAPT1
Sequence domains: FKBP12-rapamycin binding domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 57.034Å b: 67.419Å c: 69.793Å
α: 90° β: 107.2° γ: 90°
R-values:
R R work R free
0.201 0.198 0.258
Expression system: Escherichia coli