1PBK: Homologous domain of human FKBP25

Homologous domain of human FKBP25. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Oct 1996.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,028
Mol. weight: 13.87 kDa
Ligands: RAP
Released: 14 Oct 1996

Explore 1PBK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PBK contains 5 α-helices and 8 β-strands across 1 chain. 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
α-helix	160-161	2
β-strand	162-165	4	1
α-helix	173-179	7
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
FKBP25	A	protein	116	Homo sapiens	Q00688 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1PBK_1 FKBP25 (chains A)
PKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGV
GKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID

Ligands and cofactors

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

Primary citation

Structure of the human 25 kDa FK506 binding protein complexed with rapamycin. Liang, J., Hung, D.T., Schreiber, S.L. et al. J Am Chem Soc (1996) 118:1231-1232. PubMed

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

5GPG 1.67 Å, Co-crystal structure of the FK506 binding domain of human FKBP25, Rapamycin and the FRB…
5D75 1.83 Å, Crystal structure of Human FKBD25 in complex with FK506
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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