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1OK8

Crystal structure of the dengue 2 virus envelope glycoprotein in the postfusion conformation

Summary for 1OK8
Entry DOI10.2210/pdb1ok8/pdb
Related1L9K 1OAM 1OAN
DescriptorMAJOR ENVELOPE PROTEIN E, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsviral protein, membrane fusion, flavivirus, fusion peptide, low-ph conformational change, class 2 fusion protein
Biological sourceDENGUE VIRUS TYPE 2
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): P12823
Total number of polymer chains1
Total formula weight44076.05
Authors
Modis, Y.,Harrison, S.C. (deposition date: 2003-07-19, release date: 2004-01-29, Last modification date: 2023-12-13)
Primary citationModis, Y.,Ogata, S.,Clements, D.,Harrison, S.C.
Structure of the Dengue Virus Envelope Protein After Membrane Fusion
Nature, 427:313-, 2004
Cited by
PubMed: 14737159
DOI: 10.1038/NATURE02165
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

217705

数据于2024-03-27公开中

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