4DRQ: Peptidyl-prolyl cis-trans isomerase FKBP5

Name: PDB 4DRQ: Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimet…
Published: 2012-04-18
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acid. Determined by X-ray diffraction at 1.0 Å resolution. Released 18 Apr 2012.

Method: X-ray diffraction
Resolution: 1.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,341
Mol. weight: 14.69 kDa
Ligands: 0OS
Released: 18 Apr 2012

Explore 4DRQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4DRQ contains 6 α-helices and 9 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: 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	47-48	2
β-strand	52-61	10	1
β-strand	66-69	4	1
α-helix	71-73	3
β-strand	77-80	4	1
α-helix	88-95	8
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

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>4DRQ_1 Peptidyl-prolyl cis-trans isomerase FKBP5 (chains A)
GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHD
RNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEI
ELLDFKGE

Ligands and cofactors

ID	Name	Formula	Copies
0OS	{3-[(1S)-1-[({(2S)-1-[(3,5-dichlorophenyl)sulfonyl]piperidin-2-yl}carbonyl)oxy]…	C31 H33 Cl2 N O9 S	1

Primary citation

Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52. Gopalakrishnan, R., Kozany, C., Wang, Y. et al. J Med Chem (2012) 55:4123-4131. DOI 10.1021/jm201747c · 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
7APS 0.94 Å, The Fk1 domain of FKBP51 in complex with (2S)-2-((1S,5R,6R)-10-((3,5-dichlorophenyl)sulfo…
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
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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