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TargetActivin receptor type-1
LigandBDBM451816
Substrate/Competitorn/a
Meas. Tech.ChEMBL_2219788 (CHEMBL5133122)
IC50 3.6±n/a nM
Citation Witten, MRWu, LLai, CTKapilashrami, KPusey, MGallagher, KChen, YYao, W Inhibition of ALK2 with bicyclic pyridyllactams. Bioorg Med Chem Lett55:0 (2022) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Activin receptor type-1
Name:Activin receptor type-1
Synonyms:2.7.11.30 | ACTR-I | ACVR1 | ACVR1_HUMAN | ACVRLK2 | ALK-2 | ALK2/ACVR1 | Activin receptor type I | Activin receptor-like kinase 2 | Activin receptor-like kinase 2 (ALK-2) | Activin receptor-like kinase 2 (ALK2/ACVR1) | Q04771 | SKR1 | Serine/threonine-protein kinase receptor R1 | TGF-B superfamily receptor type I | TSR-I
Type:n/a
Mol. Mass.:57158.32
Organism:Homo sapiens (Human)
Description:n/a
Residue:509
Sequence:
MVDGVMILPVLIMIALPSPSMEDEKPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSIN
DGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNF
HLEVGLIILSVVFAVCLLACLLGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTL
ADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSR
DEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTL
DTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVM
HSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVS
NGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQ
NPSARLTALRIKKTLTKIDNSLDKLKTDC
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM451816
n/a
NameBDBM451816
Synonyms:US10710980, Example 46 | US10947218, Example 46
TypeSmall organic molecule
Emp. Form.C25H33FN4O2
Mol. Mass.440.5535
SMILESC[C@@H]1CCCN1Cc1ccc(cc1F)-c1cnc(N)c(c1)C(=O)N[C@H]1CC[C@](C)(O)CC1 |r,wU:24.26,27.30,1.0,wD:27.31,(4.77,-2.71,;6.24,-3.19,;6.71,-4.65,;8.25,-4.65,;8.73,-3.19,;7.48,-2.28,;7.48,-.74,;6.15,.03,;4.81,-.74,;3.48,.03,;3.48,1.57,;4.81,2.34,;6.15,1.57,;7.48,2.34,;2.15,2.34,;2.15,3.88,;.81,4.65,;-.52,3.88,;-1.85,4.65,;-.52,2.34,;.81,1.57,;-1.85,1.57,;-1.85,.03,;-3.19,2.34,;-4.52,1.57,;-4.52,.03,;-5.85,-.74,;-7.19,.03,;-7.96,-1.3,;-8.73,.03,;-7.19,1.57,;-5.85,2.34,)|
Structure
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