7APS: The Fk1 domain of FKBP51

The Fk1 domain of FKBP51 in complex with (2S)-2-((1S,5R,6R)-10-((3,5-dichlorophenyl)sulfonyl)-2-oxo-5-vinyl-3,10-diazabicyclo[4.3.1]decan-3-yl)propanoic acid. Determined by X-ray diffraction at 0.94 Å resolution. Released 3 Nov 2021.

Method: X-ray diffraction
Resolution: 0.94 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,555
Mol. weight: 28.98 kDa
Ligands: RR5
Released: 3 Nov 2021

Explore 7APS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7APS contains 11 α-helices and 18 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: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	14-21	8
β-strand	23-24	2	1
β-strand	33-39	7	1
α-helix	46-48	3
β-strand	52-60	9	1
β-strand	66-69	4	1
α-helix	70-73	4
β-strand	77-80	4	1
α-helix	88-94	7
α-helix	97-98	2
β-strand	102-107	6	1
α-helix	109-111	3
β-strand	118	1	2
β-strand	122	1	2
β-strand	128-138	11	1

Chain B: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	14-21	8
β-strand	23-24	2	3
β-strand	33-39	7	3
α-helix	47-48	2
β-strand	52-61	10	3
β-strand	66-69	4	3
β-strand	77-80	4	3
α-helix	88-94	7
α-helix	97-98	2
β-strand	102-107	6	3
α-helix	109-111	3
β-strand	118	1	4
β-strand	122	1	4
β-strand	128-138	11	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP5	A, B	protein	128	Homo sapiens	Q13451 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7APS_1 Peptidyl-prolyl cis-trans isomerase FKBP5 (chains A, B)
GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHD
RNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEI
ELLDFKGE

Ligands and cofactors

ID	Name	Formula	Copies
RR5	(2~{S})-2-[(1~{S},5~{S},6~{R})-10-[3,5-bis(chloranyl)phenyl]sulfonyl-5-ethyl-2-…	C19 H24 Cl2 N2 O5 S	2

Primary citation

Picomolar FKBP inhibitors enabled by a single water-displacing methyl group in bicyclic [4.3.1] aza-amides. Kolos, J.M., Pomplun, S., Jung, S. et al. Chem Sci (2021) 12:14758-14765. DOI 10.1039/d1sc04638a · PubMed

Other PDB entries of the same protein (UniProt Q13451 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7AOT 0.85 Å, The Fk1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphe…
7APW 0.89 Å, The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]thiazol-6-ylsulfonyl)-5-(…
8R5K 0.89 Å, The Fk1 domain of FKBP51 in complex with Antascomicine B
3O5Q 0.96 Å, Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO
6TX6 0.98 Å, Crystal structure of human FKBP51 FK1 domain A19T mutant in complex with nicotinamide
8CHN 0.99 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfonimi…
3O5P 1.0 Å, Fk1 domain mutant A19T of FKBP51, crystal form IV
4DRQ 1.0 Å, Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and…
5OBK 1.0 Å, The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(…
8CHP 1.0 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)…
8CHQ 1.01 Å, The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-3,5-dichloro-N-methylphenylsu…
4JFM 1.02 Å, Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by…

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