Structural polyprotein

Organism:

Semliki forest virus (SFV)

Uniprot:

P03315go to UniProt

Biological function:

Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell via host VLDLR or LRP8 and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:34929721). This E1 trimer is fusion active, ... [show more]go to UniProt

Representative structures for UniProt P03315

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PDB 8ihp chain I (observed residues)
PDB 8ihp chain I (observed residues)
PDB 8ua8 chain C (observed residues)
PDB 8ua8 chain C (observed residues)
PDB 8ihp chain J (observed residues)
PDB 8ihp chain J (observed residues)
PDB 8ua8 chain A (observed residues)
PDB 8ua8 chain A (observed residues)

PDB chain shown: 8ihp I go to PDBe

UniProt residues 106 - 267

Coverage: 13%

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18
Structures

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12
Ligands

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2
Interactions

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Annotations

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5
Similarity

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206
Publications

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Processed Proteins (6):

Protein Name
Representative Structures
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Available Structural Data
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Capsid protein
UniProt range of the processed protein: 1 - 267
UniProt range of representative PDB 8ihp chain I: 106 - 267
 13 Number of PDB structures
 4 Number of ligands
 1 Number of interaction partners
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Precursor of protein E3/E2
UniProt range of the processed protein: 268 - 755
UniProt range of representative PDB 8ua8 chain C: 273 - 326
 10 Number of PDB structures
 3 Number of ligands
 1 Number of interaction partners
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Assembly protein E3
UniProt range of the processed protein: 268 - 333
UniProt range of representative PDB 8ua8 chain C: 273 - 326
 6 Number of PDB structures
 3 Number of ligands
 1 Number of interaction partners
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Spike glycoprotein E2
UniProt range of the processed protein: 334 - 755
UniProt range of representative PDB 8ihp chain J: 334 - 755
 10 Number of PDB structures
 3 Number of ligands
 1 Number of interaction partners
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