Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB08073"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"(2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE"
|
| rdf:type | |
| drugbank:description |
"
experimental
This compound belongs to the tryptamines and derivatives. These are compounds containing the tryptamine backbone, which is structurally characterized by an indole ring subsituted at the thrid position by an ethanamine.
Tryptamines and Derivatives
Organic Compounds
Heterocyclic Compounds
Indoles and Derivatives
Tryptamines and Derivatives
Indoles
Indazoles
Alkyl Aryl Ethers
Substituted Pyrroles
Pyridines and Derivatives
Benzene and Substituted Derivatives
Pyrazoles
Polyamines
Monoalkylamines
indole
benzopyrazole
indazole
alkyl aryl ether
pyridine
benzene
substituted pyrrole
pyrrole
azole
pyrazole
polyamine
ether
amine
primary amine
primary aliphatic amine
organonitrogen compound
logP
3.72
ALOGPS
logS
-5.4
ALOGPS
Water Solubility
1.72e-03 g/l
ALOGPS
logP
3.07
ChemAxon
IUPAC Name
5-{5-[(2S)-2-amino-3-(1H-indol-3-yl)propoxy]pyridin-3-yl}-3-methyl-1H-indazole
ChemAxon
Traditional IUPAC Name
5-{5-[(2S)-2-amino-3-(1H-indol-3-yl)propoxy]pyridin-3-yl}-3-methyl-1H-indazole
ChemAxon
Molecular Weight
397.4723
ChemAxon
Monoisotopic Weight
397.190260383
ChemAxon
SMILES
[H][C@@](N)(COC1=CN=CC(=C1)C1=CC=C2NN=C(C)C2=C1)CC1=CNC2=CC=CC=C12
ChemAxon
Molecular Formula
C24H23N5O
ChemAxon
InChI
InChI=1S/C24H23N5O/c1-15-22-10-16(6-7-24(22)29-28-15)17-9-20(13-26-11-17)30-14-19(25)8-18-12-27-23-5-3-2-4-21(18)23/h2-7,9-13,19,27H,8,14,25H2,1H3,(H,28,29)/t19-/m0/s1
ChemAxon
InChIKey
InChIKey=YWTBGJGMTBHQTM-IBGZPJMESA-N
ChemAxon
Polar Surface Area (PSA)
92.61
ChemAxon
Refractivity
118.18
ChemAxon
Polarizability
44.51
ChemAxon
Rotatable Bond Count
6
ChemAxon
H Bond Acceptor Count
4
ChemAxon
H Bond Donor Count
3
ChemAxon
pKa (strongest acidic)
14.17
ChemAxon
pKa (strongest basic)
9.24
ChemAxon
Physiological Charge
1
ChemAxon
Number of Rings
5
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
MDDR-Like Rule
true
ChemAxon
PubChem Compound
10172943
PubChem Substance
99444544
ChemSpider
8348448
PDB
L20
BE0001172
RAC-beta serine/threonine-protein kinase
Human
# 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. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
RAC-beta serine/threonine-protein kinase
Involved in protein serine/threonine kinase activity
General protein kinase capable of phosphorylating several known proteins
AKT2
19q13.1-q13.2
None
6.31
55769.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:392
GenAtlas
AKT2
GeneCards
AKT2
GenBank Gene Database
M77198
GenBank Protein Database
337491
UniProtKB
P31751
UniProt Accession
AKT2_HUMAN
EC 2.7.11.1
PKB beta
Protein kinase Akt-2
Protein kinase B, beta
RAC-PK-beta
>RAC-beta serine/threonine-protein kinase
MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAEC
QLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPM
DYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAM
KILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFH
LSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEG
ISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFE
LILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQK
KLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIR
E
>1446 bp
ATGAATGAGGTGTCTGTCATCAAAGAAGGCTGGCTCCACAAGCGTGGTGAATACATCAAG
ACCTGGAGGCCACGGTACTTCCTGCTGAAGAGCGACGGCTCCTTCATTGGGTACAAGGAG
AGGCCCGAGGCCCCTGATCAGACTCTACCCCCCTTAAACAACTTCTCCGTAGCAGAATGC
CAGCTGATGAAGACCGAGAGGCCGCGACCCAACACCTTTGTCATACGCTGCCTGCAGTGG
ACCACAGTCATCGAGAGGACCTTCCACGTGGATTCTCCAGACGAGAGGGAGGAGTGGATG
CGGGCCATCCAGATGGTCGCCAACAGCCTCAAGCAGCGGGCCCCAGGCGAGGACCCCATG
GACTACAAGTGTGGCTCCCCCAGTGACTCCTCCACGACTGAGGAGATGGAAGTGGCGGTC
AGCAAGGCACGGGCTAAAGTGACCATGAATGACTTCGACTATCTCAAACTCCTTGGCAAG
GGAACCTTTGGCAAAGTCATCCTGGTGCGGGAGAAGGCCACTGGCCGCTACTACGCCATG
AAGATCCTGCGAAAGGAAGTCATCATTGCCAAGGATGAAGTCGCTCACACAGTCACCGAG
AGCCGGGTCCTCCAGAACACCAGGCACCCGTTCCTCACTGCGCTGAAGTATGCCTTCCAG
ACCCACGACCGCCTGTGCTTTGTGATGGAGTATGCCAACGGGGGTGAGCTGTTCTTCCAC
CTGTCCCGGGAGCGTGTCTTCACAGAGGAGCGGGCCCGGTTTTATGGTGCAGAGATTGTC
TCGGCTCTTGAGTACTTGCACTCGCGGGACGTGGTATACCGCGACATCAAGCTGGAAAAC
CTCATGCTGGACAAAGATGGCCACATCAAGATCACTGACTTTGGCCTCTGCAAAGAGGGC
ATCAGTGACGGGGCCACCATGAAAACCTTCTGTGGGACCCCGGAGTACCTGGCGCCTGAG
GTGCTGGAGGACAATGACTATGGCCGGGCCGTGGACTGGTGGGGGCTGGGTGTGGTCATG
TACGAGATGATGTGCGGCCGCCTGCCCTTCTACAACCAGGACCACGAGCGCCTCTTCGAG
CTCATCCTCATGGAAGAGATCCGCTTCCCGCGCACGCTCAGCCCCGAGGCCAAGTCCCTG
CTTGCTGGGCTGCTTAAGAAGGACCCCAAGCAGAGGCTTGGTGGGGGGCCCAGCGATGCC
AAGGAGGTCATGGAGCACAGGTTCTTCCTCAGCATCAACTGGCAGGACGTGGTCCAGAAG
AAGCTCCTGCCACCCTTCAAACCTCAGGTCACGTCCGAGGTCGACACAAGGTACTTCGAT
GATGAATTTACCGCCCAGTCCATCACAATCACACCCCCTGACCGCTATGACAGCCTGGGC
TTACTGGAGCTGGACCAGCGGACCCACTTCCCCCAGTTCTCCTACTCGGCCAGCATCCGC
GAGTGA
PF00169
PH
PF00069
Pkinase
PF00433
Pkinase_C
function
ATP binding
function
catalytic activity
function
transferase activity, transferring phosphorus-containing groups
function
kinase activity
function
protein kinase activity
function
protein serine/threonine kinase activity
function
nucleotide binding
function
purine nucleotide binding
function
adenyl nucleotide binding
function
binding
function
transferase activity
process
physiological process
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
process
protein amino acid phosphorylation
process
biopolymer modification
process
protein modification
BE0001065
Glycogen synthase kinase-3 beta
Human
# 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. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Glycogen synthase kinase-3 beta
Involved in protein kinase activity
Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA
GSK3B
3q13.3
None
8.97
46745.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4617
GenAtlas
GSK3B
GeneCards
GSK3B
GenBank Gene Database
L33801
GenBank Protein Database
529237
UniProtKB
P49841
UniProt Accession
GSK3B_HUMAN
EC 2.7.11.26
GSK-3 beta
>Glycogen synthase kinase-3 beta
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK
VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG
EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR
DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV
WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP
WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF
NFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST
>1263 bp
ATGTCAGGGCGGCCCAGAACCACCTCCTTTGCGGAGAGCTGCAAGCCGGTGCAGCAGCCT
TCAGCTTTTGGCAGCATGAAAGTTAGCAGAGACAAGGACGGCAGCAAGGTGACAACAGTG
GTGGCAACTCCTGGGCAGGGTCCAGACAGGCCACAAGAAGTCAGCTATACAGACACTAAA
GTGATTGGAAATGGATCATTTGGTGTGGTATATCAAGCCAAACTTTGTGATTCAGGAGAA
CTGGTCGCCATCAAGAAAGTATTGCAGGACAAGAGATTTAAGAATCGAGAGCTCCAGATC
ATGAGAAAGCTAGATCACTGTAACATAGTCCGATTGCGTTATTTCTTCTACTCCAGTGGT
GAGAAGAAAGATGAGGTCTATCTTAATCTGGTGCTGGACTATGTTCCGGAAACAGTATAC
AGAGTTGCCAGACACTATAGTCGAGCCAAACAGACGCTCCCTGTGATTTATGTCAAGTTG
TATATGTATCAGCTGTTCCGAAGTTTAGCCTATATCCATTCCTTTGGAATCTGCCATCGG
GATATTAAACCGCAGAACCTCTTGTTGGATCCTGATACTGCTGTATTAAAACTCTGTGAC
TTTGGAAGTGCAAAGCAGCTGGTCCGAGGAGAACCCAATGTTTCGTATATCTGTTCTCGG
TACTATAGGGCACCAGAGTTGATCTTTGGAGCCACTGATTATACCTCTAGTATAGATGTA
TGGTCTGCTGGCTGTGTGTTGGCTGAGCTGTTACTAGGACAACCAATATTTCCAGGGGAT
AGTGGTGTGGATCAGTTGGTAGAAATAATCAAGGTCCTGGGAACTCCAACAAGGGAGCAA
ATCAGAGAAATGAACCCAAACTACACAGAATTTAAATTCCCTCAAATTAAGGCACATCCT
TGGACTAAGGTCTTCCGACCCCGAACTCCACCGGAGGCAATTGCACTGTGTAGCCGTCTG
CTGGAGTATACACCAACTGCCCGACTAACACCACTGGAAGCTTGTGCACATTCATTTTTT
GATGAATTACGGGACCCAAATGTCAAACATCCAAATGGGCGAGACACACCTGCACTCTTC
AACTTCACCACTCAAGAACTGTCAAGTAATCCACCTCTGGCTACCATCCTTATTCCTCCT
CATGCTCGGATTCAAGCAGCTGCTTCAACCCCCACAAATGCCACAGCAGCGTCAGATGCT
AATACTGGAGACCGTGGACAGACCAATAATGCTGCTTCTGCATCAGCTTCCAACTCCACC
TGA
PF00069
Pkinase
function
catalytic activity
function
transferase activity, transferring phosphorus-containing groups
function
kinase activity
function
protein kinase activity
function
protein serine/threonine kinase activity
function
nucleotide binding
function
purine nucleotide binding
function
adenyl nucleotide binding
function
binding
function
transferase activity
function
ATP binding
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
process
protein amino acid phosphorylation
process
biopolymer modification
process
protein modification
process
physiological process
BE0003761
cAMP-dependent protein kinase catalytic subunit alpha
Human
# 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. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
cAMP-dependent protein kinase catalytic subunit alpha
Involved in ATP binding
Phosphorylates a large number of substrates in the cytoplasm and the nucleus
PRKACA
19p13.1
Cytoplasm (By similarity). Nucleus (By similarity)
None
9.22
40589.4
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:9380
GeneCards
PRKACA
GenBank Gene Database
X07767
GenBank Protein Database
35479
UniProtKB
P17612
UniProt Accession
KAPCA_HUMAN
PKA C-alpha
>cAMP-dependent protein kinase catalytic subunit alpha
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML
VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>1056 bp
ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA
GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC
TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG
GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG
GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC
TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC
ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT
GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG
CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC
ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC
GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG
GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC
GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC
CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG
CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA
ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA
GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC
AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG
PF00069
Pkinase
function
ATP binding
function
catalytic activity
function
transferase activity, transferring phosphorus-containing groups
function
kinase activity
function
protein kinase activity
function
protein serine/threonine kinase activity
function
nucleotide binding
function
purine nucleotide binding
function
adenyl nucleotide binding
function
binding
function
transferase activity
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
process
protein amino acid phosphorylation
process
biopolymer modification
process
protein modification
process
physiological process
BE0003762
cAMP-dependent protein kinase inhibitor alpha
Human
# 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. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
cAMP-dependent protein kinase inhibitor alpha
Involved in cAMP-dependent protein kinase inhibitor act
Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains
PKIA
8q21.12
None
4.18
7988.4
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:9017
GeneCards
PKIA
GenBank Gene Database
S76965
GenBank Protein Database
243494
UniProtKB
P61925
UniProt Accession
IPKA_HUMAN
cAMP-dependent protein kinase inhibitor, muscle/brain isoform
PKI-alpha
>cAMP-dependent protein kinase inhibitor alpha
MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS
TEQSGEAQGEAAKSES
>231 bp
ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA
AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG
AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT
ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA
PF02827
PKI
function
enzyme regulator activity
function
enzyme inhibitor activity
function
kinase inhibitor activity
function
protein kinase inhibitor activity
function
cAMP-dependent protein kinase inhibitor activity
process
regulation of kinase activity
process
regulation of protein kinase activity
process
negative regulation of protein kinase activity
process
regulation of biological process
process
regulation of enzyme activity
process
regulation of transferase activity
"
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All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
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