The structure of the folded domain of the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.
External Resource: Annotation
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
B | SCOP2B Superfamily | ICP27-like | 8093036 | 3002668 | SCOP2B (2022-06-29) |
A | SCOP2 Family | ICP27-like | 8047240 | 4005522 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | ICP27-like | 8093036 | 3002668 | SCOP2 (2022-06-29) |
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
B | Herpes_UL69 | e4yxpB1 | A: alpha duplicates or obligate multimers | X: ICP27 homology domain (From Topology) | H: ICP27 homology domain (From Topology) | T: ICP27 homology domain | F: Herpes_UL69 | ECOD (1.6) |
A | Herpes_UL69 | e4yxpA1 | A: alpha duplicates or obligate multimers | X: ICP27 homology domain (From Topology) | H: ICP27 homology domain (From Topology) | T: ICP27 homology domain | F: Herpes_UL69 | ECOD (1.6) |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| mRNA export factor | | | |