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1OAN

Crystal structure of the dengue 2 virus envelope protein

Summary for 1OAN
Entry DOI10.2210/pdb1oan/pdb
Related1OAM
DescriptorENVELOPE GLYCOPROTEIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (5 entities in total)
Functional Keywordsglycoprotein, dengue virus, membrane fusion, flavivirus, fusion peptide, low-ph conformational change
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 chains2
Total formula weight89569.55
Authors
Modis, Y.,Harrison, S.C. (deposition date: 2003-01-16, release date: 2003-05-16, Last modification date: 2023-12-13)
Primary citationModis, Y.,Ogata, S.,Clements, D.,Harrison, S.C.
A Ligand-Binding Pocket in the Dengue Virus Envelope Glycoprotein
Proc.Natl.Acad.Sci.USA, 100:6986-, 2003
Cited by
PubMed: 12759475
DOI: 10.1073/PNAS.0832193100
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

218853

數據於2024-04-24公開中

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