5GPG: Peptidyl-prolyl cis-trans isomerase FKBP3

Co-crystal structure of the FK506 binding domain of human FKBP25, Rapamycin and the FRB domain of human mTOR. Determined by X-ray diffraction at 1.67 Å resolution. Released 12 Oct 2016.

Method: X-ray diffraction
Resolution: 1.67 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,009
Mol. weight: 25.31 kDa
Ligands: RAP
Released: 12 Oct 2016

Explore 5GPG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GPG contains 10 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	111-117	7	1
β-strand	130-138	9	1
β-strand	144-147	4	1
β-strand	162-165	4	1
α-helix	173-178	6
α-helix	179-181	3
α-helix	182-183	2
β-strand	187-192	6	1
α-helix	194-196	3
β-strand	203	1	2
α-helix	204-206	3
β-strand	208	1	2
β-strand	214-223	10	1

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	2023-2035	13
α-helix	2036-2040	5
α-helix	2044-2060	17
α-helix	2065-2091	27
α-helix	2094-2110	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP3	A	protein	117	Homo sapiens	Q00688 (AlphaFold model)
Serine/threonine-protein kinase mTOR	B	protein	93	Homo sapiens	P42345 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5GPG_1 Peptidyl-prolyl cis-trans isomerase FKBP3 (chains A)
SPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVG
VGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID

Sequence of entity 2 (B), FASTA

>5GPG_2 Serine/threonine-protein kinase mTOR (chains B)
SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLM
EAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRIS

Ligands and cofactors

ID	Name	Formula	Copies
RAP	Rapamycin immunosuppressant drug	C51 H79 N O13	1

Primary citation

Proximity-Directed Labeling Reveals a New Rapamycin-Induced Heterodimer of FKBP25 and FRB in Live Cells. Lee, S.Y., Lee, H., Lee, H.K. et al. ACS Cent Sci (2016) 2:506-516. DOI 10.1021/acscentsci.6b00137 · PubMed

Other PDB entries of the same protein (UniProt Q00688 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5D75 1.83 Å, Crystal structure of Human FKBD25 in complex with FK506
1PBK 2.5 Å, Homologous domain of human FKBP25
2KFV Structure of the amino-terminal domain of human FK506-binding protein 3 / Northeast…
2MPH Solution Structure of human FK506 binding Protein 25

Browse structure collections

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