| Reaction Details |
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 | Report a problem with these data |
| Target | Cyclic GMP-AMP synthase |
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| Ligand | BDBM50250108 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1680902 (CHEMBL4031179) |
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| Kd | 200±n/a nM |
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| Citation |  Hall, J; Brault, A; Vincent, F; Weng, S; Wang, H; Dumlao, D; Aulabaugh, A; Aivazian, D; Castro, D; Chen, M; Culp, J; Dower, K; Gardner, J; Hawrylik, S; Golenbock, D; Hepworth, D; Horn, M; Jones, L; Jones, P; Latz, E; Li, J; Lin, LL; Lin, W; Lin, D; Lovering, F; Niljanskul, N; Nistler, R; Pierce, B; Plotnikova, O; Schmitt, D; Shanker, S; Smith, J; Snyder, W; Subashi, T; Trujillo, J; Tyminski, E; Wang, G; Wong, J; Lefker, B; Dakin, L; Leach, K Discovery of PF-06928215 as a high affinity inhibitor of cGAS enabled by a novel fluorescence polarization assay. PLoS ONE12:1-16 (2017) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Cyclic GMP-AMP synthase |
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| Name: | Cyclic GMP-AMP synthase |
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| Synonyms: | 2.7.7.86 | C6orf150 | CGAS | CGAS_HUMAN | Cyclic GMP-AMP synthase | MB21D1 | Mab-21 domain-containing protein 1 | Synonyms=C6orf150 | cGAMP synthase | h-cGAS |
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| Type: | PROTEIN |
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| Mol. Mass.: | 58845.55 |
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| Organism: | Homo sapiens |
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| Description: | ChEMBL_117333 |
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| Residue: | 522 |
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| Sequence: | MQPWHGKAMQRASEAGATAPKASARNARGAPMDPTESPAAPEAALPKAGKFGPARKSGSR
QKKSAPDTQERPPVRATGARAKKAPQRAQDTQPSDATSAPGAEGLEPPAAREPALSRAGS
CRQRGARCSTKPRPPPGPWDVPSPGLPVSAPILVRRDAAPGASKLRAVLEKLKLSRDDIS
TAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLE
EYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKR
KRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLV
PKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQL
KERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKL
ENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
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| BDBM50250108 |
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| n/a |
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| Name | BDBM50250108 |
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| Synonyms: | CHEMBL4096573 |
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| Type | Small organic molecule |
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| Emp. Form. | C20H20N4O4 |
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| Mol. Mass. | 380.3972 |
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| SMILES | OC(=O)[C@@H]1CCCC[C@@H]1NC(=O)c1cnn2c(O)cc(nc12)-c1ccccc1 |r| |
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| Structure | 
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