3U1J
Aprotinin bound to Dengue virus protease
Summary for 3U1J
Entry DOI | 10.2210/pdb3u1j/pdb |
Related | 3U1I |
Descriptor | Serine protease subunit NS2B, Serine protease NS3, Pancreatic trypsin inhibitor, ... (4 entities in total) |
Functional Keywords | serine protease, bovine pancreatic trypsin inhibitor, er membrane, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Dengue virus 3 (DENV-3) More |
Cellular location | Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q5UB51 Q5UB51 Secreted: P00974 |
Total number of polymer chains | 3 |
Total formula weight | 32272.02 |
Authors | Noble, C.G. (deposition date: 2011-09-30, release date: 2011-11-09, Last modification date: 2023-11-01) |
Primary citation | Noble, C.G.,Seh, C.C.,Chao, A.T.,Shi, P.Y. Ligand-bound structures of the dengue virus protease reveal the active conformation J.Virol., 86:438-446, 2012 Cited by PubMed: 22031935DOI: 10.1128/JVI.06225-11 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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