Summary for 5FFM
| Entry DOI | 10.2210/pdb5ffm/pdb |
| Descriptor | Serine protease NS3 (2 entities in total) |
| Functional Keywords | dead helicase rna triphosphatase, hydrolase |
| Biological source | Yellow fever virus (strain 17D vaccine) (YFV) |
| Cellular location | Capsid 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 : P03314 |
| Total number of polymer chains | 1 |
| Total formula weight | 50010.09 |
| Authors | Smith, J.L. (deposition date: 2015-12-18, release date: 2015-12-30, Last modification date: 2024-10-30) |
| Primary citation | Wu, J.,Bera, A.K.,Kuhn, R.J.,Smith, J.L. Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J. Virol., 79:10268-10277, 2005 Cited by PubMed Abstract: Yellow fever virus (YFV), a member of the Flavivirus genus, has a plus-sense RNA genome encoding a single polyprotein. Viral protein NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping. The 1.8-A crystal structure of the helicase region of the YFV NS3 protein includes residues 187 to 623. Two familiar helicase domains bind nucleotide in a triphosphate pocket without base recognition, providing a site for nonspecific hydrolysis of nucleoside triphosphates and RNA triphosphate. The third, C-terminal domain has a unique structure and is proposed to function in RNA and protein recognition. The organization of the three domains indicates that cleavage of the viral polyprotein NS3-NS4A junction occurs in trans. PubMed: 16051820PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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