1MDT
THE REFINED STRUCTURE OF MONOMERIC DIPHTHERIA TOXIN AT 2.3 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008320 | molecular_function | protein transmembrane transporter activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0047286 | molecular_function | NAD+-diphthamide ADP-ribosyltransferase activity |
| A | 0071806 | biological_process | protein transmembrane transport |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008320 | molecular_function | protein transmembrane transporter activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0047286 | molecular_function | NAD+-diphthamide ADP-ribosyltransferase activity |
| B | 0071806 | biological_process | protein transmembrane transport |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE APU A 901 |
| Chain | Residue |
| A | HIS21 |
| A | GLY22 |
| A | LYS24 |
| A | GLY34 |
| A | ILE35 |
| A | GLN36 |
| A | PRO38 |
| A | THR42 |
| A | GLY44 |
| A | PHE53 |
| A | TYR54 |
| A | TYR65 |
| A | TRP153 |
| A | SER446 |
| A | ARG458 |
| A | HOH538 |
| A | HOH539 |
| A | HOH586 |
| A | HOH588 |
| A | HOH590 |
| A | HOH667 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE APU B 901 |
| Chain | Residue |
| B | HIS21 |
| B | GLY22 |
| B | LYS24 |
| B | TYR27 |
| B | ILE31 |
| B | GLY34 |
| B | ILE35 |
| B | GLN36 |
| B | THR42 |
| B | GLY44 |
| B | ASN45 |
| B | TYR54 |
| B | TYR65 |
| B | TRP153 |
| B | SER446 |
| B | ARG458 |
| B | HOH906 |
| B | HOH951 |
| B | HOH953 |
| B | HOH955 |
| B | HOH975 |
| B | HOH1003 |
| B | HOH1075 |
| site_id | CAT |
| Number of Residues | 5 |
| Details | CATALYTIC SITE IN CHAIN A |
| Chain | Residue |
| A | HIS21 |
| A | TYR65 |
| A | GLU148 |
| A | SER446 |
| A | ARG458 |
| site_id | CBT |
| Number of Residues | 5 |
| Details | CATALYTIC SITE IN CHAIN B |
| Chain | Residue |
| B | ARG458 |
| B | HIS21 |
| B | TYR65 |
| B | GLU148 |
| B | SER446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Modification inactivates enzyme"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tox |
| Chain | Residue | Details |
| A | GLU148 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tox |
| Chain | Residue | Details |
| B | GLU148 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 773 |
| Chain | Residue | Details |
| A | GLU148 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 773 |
| Chain | Residue | Details |
| B | GLU148 | electrostatic stabiliser |
