6NAE
Crystal Structure of Ebola zaire GP protein with bound ARN0074898
Summary for 6NAE
| Entry DOI | 10.2210/pdb6nae/pdb |
| Descriptor | Envelope glycoprotein,Envelope glycoprotein,Envelope glycoprotein, Envelope glycoprotein, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | ssgcid, ebola zaire, glycoprotein, structural genomics, seattle structural genomics center for infectious disease, viral protein |
| Biological source | Zaire ebolavirus (strain Mayinga-76) (ZEBOV) More |
| Total number of polymer chains | 2 |
| Total formula weight | 57847.70 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2018-12-05, release date: 2019-12-11, Last modification date: 2024-11-20) |
| Primary citation | Plewe, M.B.,Sokolova, N.V.,Gantla, V.R.,Brown, E.R.,Naik, S.,Fetsko, A.,Lorimer, D.D.,Dranow, D.M.,Smutney, H.,Bullen, J.,Sidhu, R.,Master, A.,Wang, J.,Kallel, E.A.,Zhang, L.,Kalveram, B.,Freiberg, A.N.,Henkel, G.,McCormack, K. Discovery of Adamantane Carboxamides as Ebola Virus Cell Entry and Glycoprotein Inhibitors. Acs Med.Chem.Lett., 11:1160-1167, 2020 Cited by PubMed Abstract: We identified and explored the structure-activity-relationship (SAR) of an adamantane carboxamide chemical series of Ebola virus (EBOV) inhibitors. Selected analogs exhibited half-maximal inhibitory concentrations (EC values) of ∼10-15 nM in (VSV) pseudotyped EBOV (pEBOV) infectivity assays, low hundred nanomolar EC activity against wild type EBOV, aqueous solubility >20 mg/mL, and attractive metabolic stability in human and nonhuman liver microsomes. X-ray cocrystallographic characterizations of a lead compound with the EBOV glycoprotein (GP) established the EBOV GP as a target for direct compound inhibitory activity and further provided relevant structural models that may assist in identifying optimized therapeutic candidates. PubMed: 32550996DOI: 10.1021/acsmedchemlett.0c00025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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