1TOX
DIPHTHERIA TOXIN DIMER COMPLEXED WITH NAD
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 | 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 | 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 | 15 |
Details | BINDING SITE FOR RESIDUE NAD A 536 |
Chain | Residue |
A | SER55 |
A | TYR65 |
A | GLU148 |
A | TRP153 |
A | ARG458 |
A | HOH649 |
A | HOH673 |
A | HOH683 |
A | HIS21 |
A | GLY22 |
A | THR23 |
A | GLY34 |
A | ILE35 |
A | GLN36 |
A | TYR54 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NAD B 536 |
Chain | Residue |
B | HIS21 |
B | GLY22 |
B | THR23 |
B | TYR27 |
B | GLY34 |
B | ILE35 |
B | GLN36 |
B | TYR54 |
B | TYR65 |
B | GLU148 |
B | HOH612 |
site_id | CAA |
Number of Residues | 1 |
Details |
Chain | Residue |
A | GLU148 |
site_id | CAB |
Number of Residues | 1 |
Details |
Chain | Residue |
B | GLU148 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLN155 | |
B | GLN155 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | VAL28 | |
A | PRO72 | |
B | VAL28 | |
B | PRO72 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Modification inactivates enzyme |
Chain | Residue | Details |
A | SER160 | |
B | SER160 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Cleavage; by furin => ECO:0000269|PubMed:8253774 |
Chain | Residue | Details |
A | SER200 | |
B | SER200 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 9012663, 1980208, 14756556 |
Chain | Residue | Details |
A | GLU148 |
site_id | CSA2 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 9012663, 1980208, 14756556 |
Chain | Residue | Details |
B | GLU148 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 773 |
Chain | Residue | Details |
A | GLN155 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 773 |
Chain | Residue | Details |
B | GLN155 | electrostatic stabiliser |