Drug Interactions: This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Not Available
Food Interactions: Not Available

Chemical Identifiers

UNII: 55H1ZOI1NL
CAS number: 171009-07-7
InChI Key: OWPMENVYXDJDOW-UHFFFAOYSA-N
InChI: InChI=1S/C20H20N2O4/c1-3-12-8-14(16(24)10-15(12)23)20-19(11(2)21-22-20)13-4-5-17-18(9-13)26-7-6-25-17/h4-5,8-10,23-24H,3,6-7H2,1-2H3,(H,21,22)
IUPAC Name: 4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-3-methyl-1H-pyrazol-5-yl]-6-ethylbenzene-1,3-diol
SMILES: CCC1=C(O)C=C(O)C(=C1)C1=C(C(C)=NN1)C1=CC2=C(OCCO2)C=C1

References

General References

Not Available

External Links

PubChem Compound: 5327091
PubChem Substance: 99444065
ChemSpider: 10392116
BindingDB: 15362
ChEBI: 41656
ChEMBL: CHEMBL399530
ZINC: ZINC000008536348
PDBe Ligand: CT5

PDB Entries

2brc / 2bt0

Clinical Trials

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Pharmacoeconomics

Manufacturers: Not Available
Packagers: Not Available
Dosage Forms: Not Available
Prices: Not Available
Patents: Not Available

Properties

State

Solid

Experimental Properties

Not Available

Predicted Properties

Property	Value	Source
Water Solubility	0.104 mg/mL	ALOGPS
logP	3.61	ALOGPS
logP	3.49	Chemaxon
logS	-3.5	ALOGPS
pKa (Strongest Acidic)	9.21	Chemaxon
pKa (Strongest Basic)	3.07	Chemaxon
Physiological Charge	0	Chemaxon
Hydrogen Acceptor Count	5	Chemaxon
Hydrogen Donor Count	3	Chemaxon
Polar Surface Area	87.6 Å²	Chemaxon
Rotatable Bond Count	3	Chemaxon
Refractivity	99.05 m³·mol^-1	Chemaxon
Polarizability	37.26 Å³	Chemaxon
Number of Rings	4	Chemaxon
Bioavailability	1	Chemaxon
Rule of Five	Yes	Chemaxon
Ghose Filter	Yes	Chemaxon
Veber's Rule	No	Chemaxon
MDDR-like Rule	No	Chemaxon

Predicted ADMET Features

Property	Value	Probability
Human Intestinal Absorption	+	0.9964
Blood Brain Barrier	+	0.6516
Caco-2 permeable	-	0.6324
P-glycoprotein substrate	Non-substrate	0.5299
P-glycoprotein inhibitor I	Non-inhibitor	0.8841
P-glycoprotein inhibitor II	Non-inhibitor	0.9652
Renal organic cation transporter	Non-inhibitor	0.8364
CYP450 2C9 substrate	Non-substrate	0.8757
CYP450 2D6 substrate	Non-substrate	0.7756
CYP450 3A4 substrate	Non-substrate	0.5103
CYP450 1A2 substrate	Inhibitor	0.7708
CYP450 2C9 inhibitor	Inhibitor	0.572
CYP450 2D6 inhibitor	Non-inhibitor	0.8608
CYP450 2C19 inhibitor	Inhibitor	0.5642
CYP450 3A4 inhibitor	Non-inhibitor	0.6608
CYP450 inhibitory promiscuity	High CYP Inhibitory Promiscuity	0.7427
Ames test	AMES toxic	0.5145
Carcinogenicity	Non-carcinogens	0.8781
Biodegradation	Not ready biodegradable	1.0
Rat acute toxicity	2.3374 LD50, mol/kg	Not applicable
hERG inhibition (predictor I)	Weak inhibitor	0.8997
hERG inhibition (predictor II)	Non-inhibitor	0.7112

ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)

Not Available

Spectra

Spectrum	Spectrum Type	Splash Key
Predicted MS/MS Spectrum - 10V, Positive (Annotated)	Predicted LC-MS/MS	splash10-0udi-0009000000-97fd2ffc48e21d06db12
Predicted MS/MS Spectrum - 10V, Negative (Annotated)	Predicted LC-MS/MS	splash10-0udi-0009000000-8223649cdd08477f843e
Predicted MS/MS Spectrum - 20V, Positive (Annotated)	Predicted LC-MS/MS	splash10-0zg0-0019000000-1e0eb49fdcd8ad4e09df
Predicted MS/MS Spectrum - 20V, Negative (Annotated)	Predicted LC-MS/MS	splash10-00di-0009000000-9891562ea5ff55daba3d
Predicted MS/MS Spectrum - 40V, Negative (Annotated)	Predicted LC-MS/MS	splash10-00di-0029000000-27d36b465cdca60f64cb
Predicted MS/MS Spectrum - 40V, Positive (Annotated)	Predicted LC-MS/MS	splash10-056r-0039000000-5a5dc787c2b7e4d6bba2
Predicted 1H NMR Spectrum	1D NMR	Not Applicable
Predicted 13C NMR Spectrum	1D NMR	Not Applicable

Chromatographic Properties

Collision Cross Sections (CCS)

Adduct	CCS Value (Å²)	Source type	Source
[M-H]-	185.315	predicted	DeepCCS 1.0 (2019)
[M+H]+	187.673	predicted	DeepCCS 1.0 (2019)
[M+Na]+	194.80669	predicted	DeepCCS 1.0 (2019)

Targets

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Details1. Heat shock protein HSP 90-alpha

Kind: Protein
Organism: Humans
Pharmacological action: Yes
Actions: Inhibitor

General Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812)
Specific Function: ATP binding
Gene Name: HSP90AA1
Uniprot ID: P07900
Uniprot Name: Heat shock protein HSP 90-alpha
Molecular Weight: 84659.015 Da

References

Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]

Details2. Heat shock protein HSP 90-beta

Kind: Protein
Organism: Humans
Pharmacological action: Unknown

General Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)
Specific Function: ATP binding
Gene Name: HSP90AB1
Uniprot ID: P08238
Uniprot Name: Heat shock protein HSP 90-beta
Molecular Weight: 83263.475 Da

References

Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]

Drug created at September 15, 2010 21:23 / Updated at August 26, 2024 19:22

CCT-018159

Identification

Structure for CCT-018159 (DB07594)

Pharmacology

Interactions

Categories

Chemical Identifiers

References

Clinical Trials

Clinical Trial & Rare Diseases Add-on Data Package

Pharmacoeconomics

Properties

Spectra

Collision Cross Sections (CCS)

Targets

References

References