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3U1I

Dengue virus protease covalently bound to a peptide

Summary for 3U1I
Entry DOI10.2210/pdb3u1i/pdb
Related3UIJ
Related PRD IDPRD_000988
DescriptorSerine protease subunit NS2B, Serine protease NS3, peptide of (BEZ)(NLE)KR(OAR), ... (5 entities in total)
Functional Keywordsserine protease, er membrane, viral protein, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceDengue virus 3 (DENV-3)
More
Cellular locationCapsid 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
Total number of polymer chains6
Total formula weight53200.87
Authors
Noble, C.G. (deposition date: 2011-09-29, release date: 2011-11-09, Last modification date: 2023-11-15)
Primary citationNoble, 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: 22031935
DOI: 10.1128/JVI.06225-11
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

217705

數據於2024-03-27公開中

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