5EHG
DENGUE 3 NS5 METHYLTRANSFERASE BOUND TO S-ADENOSYL METHIONINE AND MOLECULE BF341
Summary for 5EHG
Entry DOI | 10.2210/pdb5ehg/pdb |
Descriptor | RNA-directed RNA polymerase NS5, S-ADENOSYLMETHIONINE, 4-[3-[(2-azanyl-4-chloranyl-phenyl)carbamoylamino]phenyl]sulfonyloxybenzoic acid, ... (4 entities in total) |
Functional Keywords | transferase, dengue virus, ns5 methyltransferase, fragment-based drug discovery |
Biological source | Dengue virus type 3 (strain Philippines/H87/1956) (DENV-3) |
Cellular location | Protein C: Virion . Peptide pr: Secreted . Small envelope protein M: Virion membrane ; Multi-pass membrane protein . Envelope protein E: Virion membrane ; Multi-pass membrane protein . Non-structural protein 1: Secreted . Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 2A: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . Serine protease subunit NS2B: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side : P27915 |
Total number of polymer chains | 2 |
Total formula weight | 63672.37 |
Authors | Barral, K.,Bricogne, G.,Sharff, A. (deposition date: 2015-10-28, release date: 2016-10-26, Last modification date: 2024-01-10) |
Primary citation | Benmansour, F.,Trist, I.,Coutard, B.,Decroly, E.,Querat, G.,Brancale, A.,Barral, K. Discovery of novel dengue virus NS5 methyltransferase non-nucleoside inhibitors by fragment-based drug design. Eur.J.Med.Chem., 125:865-880, 2016 Cited by PubMed: 27750202DOI: 10.1016/j.ejmech.2016.10.007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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