THE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXIN
External Resource: Annotation
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
A | SCOP2B Superfamily | ADP-ribosylation | 8036997 | 3001208 | SCOP2B (2022-06-29) |
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
A | Diphtheria_C | e1dtpA1 | A: a+b complex topology | X: ADP-ribosylation (From Topology) | H: ADP-ribosylation (From Topology) | T: ADP-ribosylation | F: Diphtheria_C | ECOD (1.6) |
Chains | Accession | Name | Description | Comments | Source |
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| PF02763 | Diphtheria toxin, C domain (Diphtheria_C) | Diphtheria toxin, C domain | N-terminal catalytic (C) domain - blocks protein synthesis by transfer of ADP-ribose from NAD to a diphthamide residue of EF-2. | Domain |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| DIPHTHERIA TOXIN | | - | |