Functional Information from GO Data
| Chain | GOid | namespace | contents |
| T | 0005576 | cellular_component | extracellular region |
| T | 0005615 | cellular_component | extracellular space |
| T | 0005886 | cellular_component | plasma membrane |
| T | 0008320 | molecular_function | protein transmembrane transporter activity |
| T | 0016740 | molecular_function | transferase activity |
| T | 0016757 | molecular_function | glycosyltransferase activity |
| T | 0016779 | molecular_function | nucleotidyltransferase activity |
| T | 0035821 | biological_process | modulation of process of another organism |
| T | 0042802 | molecular_function | identical protein binding |
| T | 0047286 | molecular_function | NAD+-diphthamide ADP-ribosyltransferase activity |
| T | 0071806 | biological_process | protein transmembrane transport |
| T | 0090729 | molecular_function | toxin activity |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CiChpGyhGErC |
| Chain | Residue | Details |
| R | CYS132-CYS143 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CiChpGYhger....C |
| Chain | Residue | Details |
| R | CYS132-CYS143 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Modification inactivates enzyme"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Plays a critical role in diphtheria toxin binding and toxin sensitivity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tox |
| Chain | Residue | Details |
| T | GLU148 | |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 773 |