1PWW
Crystal structure of Anthrax Lethal Factor active site mutant protein complexed with an optimised peptide substrate in the presence of zinc.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0044164 | cellular_component | host cell cytosol |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090729 | molecular_function | toxin activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0044164 | cellular_component | host cell cytosol |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 9001 |
| Chain | Residue |
| A | HIS686 |
| A | HIS690 |
| A | TYR728 |
| A | GLU735 |
| C | PRO10 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 9002 |
| Chain | Residue |
| D | TYR9 |
| D | PRO10 |
| B | HIS686 |
| B | HIS690 |
| B | TYR728 |
| B | GLU735 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:9573135 |
| Chain | Residue | Details |
| A | CYS687 | |
| B | CYS687 |
| Chain | Residue | Details |
| A | HIS686 | |
| A | HIS690 | |
| B | HIS690 | |
| B | GLU735 | |
| A | GLU735 | |
| B | HIS686 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339 |
| Chain | Residue | Details |
| A | TYR728 | |
| B | TYR728 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 641 |
| Chain | Residue | Details |
| A | HIS686 | metal ligand |
| A | CYS687 | proton acceptor, proton donor |
| A | HIS690 | metal ligand |
| A | TYR728 | electrostatic stabiliser |
| A | GLU735 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 641 |
| Chain | Residue | Details |
| B | HIS686 | metal ligand |
| B | CYS687 | proton acceptor, proton donor |
| B | HIS690 | metal ligand |
| B | TYR728 | electrostatic stabiliser |
| B | GLU735 | metal ligand |
