1F0L
1.55 ANGSTROM CRYSTAL STRUCTURE OF WILD TYPE DIPHTHERIA TOXIN
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 701 |
| Chain | Residue |
| A | GLU142 |
| A | HIS449 |
| A | SER451 |
| A | ASN486 |
| A | HOH1066 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 702 |
| Chain | Residue |
| A | HIS391 |
| A | LYS516 |
| A | LYS526 |
| A | HOH1039 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 703 |
| Chain | Residue |
| A | ASN166 |
| A | ARG170 |
| A | HOH1342 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 704 |
| Chain | Residue |
| A | LYS24 |
| A | LYS474 |
| A | HOH1476 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 705 |
| Chain | Residue |
| B | GLU142 |
| B | HIS449 |
| B | SER451 |
| B | ASN486 |
| B | HOH1935 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 706 |
| Chain | Residue |
| B | HIS391 |
| B | LYS516 |
| B | LYS526 |
| B | HOH1908 |
| B | HOH2098 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 707 |
| Chain | Residue |
| B | PRO225 |
| B | ASN228 |
| B | HOH2412 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 708 |
| Chain | Residue |
| B | ASN166 |
| B | HOH1911 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 709 |
| Chain | Residue |
| B | LYS24 |
| B | LYS474 |
| B | APU602 |
| B | HOH1995 |
| B | HOH2173 |
| site_id | BC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE APU A 601 |
| Chain | Residue |
| A | HIS21 |
| A | GLY22 |
| A | LYS24 |
| A | TYR27 |
| A | GLY34 |
| A | ILE35 |
| A | GLN36 |
| A | THR42 |
| A | GLY44 |
| A | ASN45 |
| A | TYR54 |
| A | TYR65 |
| A | TRP153 |
| A | SER446 |
| A | ARG458 |
| A | HOH959 |
| A | HOH967 |
| A | HOH1000 |
| A | HOH1004 |
| A | HOH1030 |
| A | HOH1037 |
| A | HOH1070 |
| A | HOH1163 |
| A | HOH1199 |
| A | HOH1235 |
| A | HOH1262 |
| A | HOH1421 |
| A | HOH1503 |
| A | HOH1520 |
| site_id | BC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE APU B 602 |
| Chain | Residue |
| B | HOH1976 |
| B | HOH2007 |
| B | HOH2078 |
| B | HOH2113 |
| B | HOH2222 |
| B | HOH2403 |
| 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 | CL709 |
| B | HOH1817 |
| B | HOH1828 |
| B | HOH1838 |
| B | HOH1853 |
| B | HOH1868 |
| B | HOH1942 |
| B | HOH1951 |
| B | HOH1953 |
| site_id | CAT |
| Number of Residues | 5 |
| Details | REFERS TO CATALYTIC SITE |
| Chain | Residue |
| A | HIS21 |
| A | TYR65 |
| A | GLU148 |
| A | SER446 |
| A | ARG458 |
| site_id | CBT |
| Number of Residues | 5 |
| Details | REFERS TO CATALYTIC SITE |
| 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 | 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 | 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 |
