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TargetNAD-dependent protein deacetylase sirtuin-1
LigandBDBM50425824
Substrate/Competitorn/a
Meas. Tech.ChEMBL_937895 (CHEMBL2317035)
Kd 1300±n/a nM
Citation Zhao, XAllison, DCondon, BZhang, FGheyi, TZhang, AAshok, SRussell, MMacEwan, IQian, YJamison, JALuz, JG The 2.5Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition. J Med Chem56:963-9 (2013) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
NAD-dependent protein deacetylase sirtuin-1
Name:NAD-dependent protein deacetylase sirtuin-1
Synonyms:NAD-Dependent Deacetylase Sirtuin-1 | NAD-dependent deacetylase sirtuin 1 | NAD-dependent protein deacetylase sirtuin-1 (SIRT1) | SIR1_HUMAN | SIR2-like protein 1 | SIR2L1 | SIRT1 | Sirtuin 1 (SIRT1) | Sirtuin-1 (SIRT1) | hSIR2
Type:Developmental protein; hydrolase
Mol. Mass.:81626.66
Organism:Homo sapiens (Human)
Description:n/a
Residue:747
Sequence:
MADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREV
PAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNL
YDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRP
RIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDI
NTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIE
YFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRII
QCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPE
QFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLG
DCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSS
PERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDL
KNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSD
SEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTD
GDDQEAINEAISVKQEVTDMNYPSNKS
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  Blast E-value cutoff:
BDBM50425824
n/a
NameBDBM50425824
Synonyms:CHEMBL2312289
TypeSmall organic molecule
Emp. Form.C13H13ClN2O
Mol. Mass.248.708
SMILESNC(=O)[C@@H]1CCCc2c1[nH]c1ccc(Cl)cc21 |r|
Structure
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